4NDN
Structural insights of MAT enzymes: MATa2b complexed with SAM and PPNP
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Chains | Type | Family Name | Domain Identifier | Family Identifier | Provenance Source (Version) |
---|---|---|---|---|---|
E | SCOP2B Superfamily | SDR-like | 8088242 | 3000038 | SCOP2B (2022-06-29) |
F | SCOP2B Superfamily | SDR-like | 8088242 | 3000038 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035289 | 3000766 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035292 | 3000766 | SCOP2B (2022-06-29) |
A | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035293 | 3000766 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035289 | 3000766 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035293 | 3000766 | SCOP2B (2022-06-29) |
B | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035292 | 3000766 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035292 | 3000766 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035293 | 3000766 | SCOP2B (2022-06-29) |
C | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035289 | 3000766 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035292 | 3000766 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035293 | 3000766 | SCOP2B (2022-06-29) |
D | SCOP2B Superfamily | S-adenosylmethionine synthetase | 8035289 | 3000766 | SCOP2B (2022-06-29) |
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
E | RmlD_sub_bind | e4ndnE1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: NAD(P)-binding Rossmann-fold domains | F: RmlD_sub_bind | ECOD (1.6) |
F | RmlD_sub_bind | e4ndnF1 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: NAD(P)-binding Rossmann-fold domains | F: RmlD_sub_bind | ECOD (1.6) |
A | S-AdoMet_synt_C | e4ndnA1 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_C | ECOD (1.6) |
A | S-AdoMet_synt_M | e4ndnA2 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_M | ECOD (1.6) |
A | S-AdoMet_synt_N | e4ndnA3 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_N | ECOD (1.6) |
B | S-AdoMet_synt_C | e4ndnB1 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_C | ECOD (1.6) |
B | S-AdoMet_synt_M | e4ndnB2 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_M | ECOD (1.6) |
B | S-AdoMet_synt_N | e4ndnB3 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_N | ECOD (1.6) |
C | S-AdoMet_synt_C | e4ndnC1 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_C | ECOD (1.6) |
C | S-AdoMet_synt_M | e4ndnC2 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_M | ECOD (1.6) |
C | S-AdoMet_synt_N | e4ndnC3 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_N | ECOD (1.6) |
D | S-AdoMet_synt_C | e4ndnD1 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_C | ECOD (1.6) |
D | S-AdoMet_synt_M | e4ndnD2 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_M | ECOD (1.6) |
D | S-AdoMet_synt_N | e4ndnD3 | A: a+b two layers | X: Alpha-lytic protease prodomain-like | H: S-adenosylmethionine synthetase (From Topology) | T: S-adenosylmethionine synthetase | F: S-AdoMet_synt_N | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
E | 3.40.50.720 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | NAD(P)-binding Rossmann-like Domain | CATH (4.3.0) |
F | 3.40.50.720 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | NAD(P)-binding Rossmann-like Domain | CATH (4.3.0) |
A | 3.30.300.10 | Alpha Beta | 2-Layer Sandwich | GMP Synthetase | Chain A, domain 3 | CATH (4.3.0) |
B | 3.30.300.10 | Alpha Beta | 2-Layer Sandwich | GMP Synthetase | Chain A, domain 3 | CATH (4.3.0) |
C | 3.30.300.10 | Alpha Beta | 2-Layer Sandwich | GMP Synthetase | Chain A, domain 3 | CATH (4.3.0) |
D | 3.30.300.10 | Alpha Beta | 2-Layer Sandwich | GMP Synthetase | Chain A, domain 3 | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF04321 | RmlD substrate binding domain (RmlD_sub_bind) | RmlD substrate binding domain | L-rhamnose is a saccharide required for the virulence of some bacteria. Its precursor, dTDP-L-rhamnose, is synthesised by four different enzymes the final one of which is RmlD. The RmlD substrate binding domain is responsi ... | Domain | |
PF00438 | S-adenosylmethionine synthetase, N-terminal domain (S-AdoMet_synt_N) | S-adenosylmethionine synthetase, N-terminal domain | The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold. | Domain | |
PF02773 | S-adenosylmethionine synthetase, C-terminal domain (S-AdoMet_synt_C) | S-adenosylmethionine synthetase, C-terminal domain | The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold. | Domain | |
PF02772 | S-adenosylmethionine synthetase, central domain (S-AdoMet_synt_M) | S-adenosylmethionine synthetase, central domain | The three domains of S-adenosylmethionine synthetase have the same alpha+beta fold. | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR036291 | NAD(P)-binding domain superfamily | Homologous Superfamily | |
IPR029903 | RmlD-like substrate binding domain | Domain | |
IPR005913 | dTDP-4-dehydrorhamnose reductase family | Family | |
IPR022636 | S-adenosylmethionine synthetase superfamily | Homologous Superfamily | |
IPR022629 | S-adenosylmethionine synthetase, central domain | Domain | |
IPR022628 | S-adenosylmethionine synthetase, N-terminal | Domain | |
IPR022631 | S-adenosylmethionine synthetase, conserved site | Conserved Site | |
IPR022630 | S-adenosylmethionine synthetase, C-terminal | Domain | |
IPR002133 | S-adenosylmethionine synthetase | Family |