5LDH
STRUCTURE OF THE ACTIVE TERNARY COMPLEX OF PIG HEART LACTATE DEHYDROGENASE WITH S-LAC-NAD AT 2.7 ANGSTROMS RESOLUTION
External Resource: Annotation
Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage
Chains | Domain Info | Class | Fold | Superfamily | Family | Domain | Species | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
B | d5ldhb1 | Alpha and beta proteins (a/b) | NAD(P)-binding Rossmann-fold domains | NAD(P)-binding Rossmann-fold domains | LDH N-terminal domain-like | Lactate dehydrogenase | pig (Sus scrofa ) [TaxId: 9823 ], | SCOPe (2.08) |
B | d5ldhb2 | Alpha and beta proteins (a+b) | LDH C-terminal domain-like | LDH C-terminal domain-like | Lactate & malate dehydrogenases, C-terminal domain | Lactate dehydrogenase | pig (Sus scrofa ) [TaxId: 9823 ], | SCOPe (2.08) |
A | d5ldha1 | Alpha and beta proteins (a/b) | NAD(P)-binding Rossmann-fold domains | NAD(P)-binding Rossmann-fold domains | LDH N-terminal domain-like | Lactate dehydrogenase | pig (Sus scrofa ) [TaxId: 9823 ], | SCOPe (2.08) |
A | d5ldha2 | Alpha and beta proteins (a+b) | LDH C-terminal domain-like | LDH C-terminal domain-like | Lactate & malate dehydrogenases, C-terminal domain | Lactate dehydrogenase | pig (Sus scrofa ) [TaxId: 9823 ], | SCOPe (2.08) |
Domain Annotation: SCOP2 Classification SCOP2 Database Homepage
Domain Annotation: ECOD Classification ECOD Database Homepage
Chains | Family Name | Domain Identifier | Architecture | Possible Homology | Homology | Topology | Family | Provenance Source (Version) |
---|---|---|---|---|---|---|---|---|
B | Ldh_1_C_13 | e5ldhB1 | A: a+b complex topology | X: LDH C-terminal domain-like (From Topology) | H: LDH C-terminal domain-like (From Topology) | T: LDH C-terminal domain-like | F: Ldh_1_C_13 | ECOD (1.6) |
B | Ldh_1_N | e5ldhB2 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: NAD(P)-binding Rossmann-fold domains | F: Ldh_1_N | ECOD (1.6) |
A | Ldh_1_C_13 | e5ldhA3 | A: a+b complex topology | X: LDH C-terminal domain-like (From Topology) | H: LDH C-terminal domain-like (From Topology) | T: LDH C-terminal domain-like | F: Ldh_1_C_13 | ECOD (1.6) |
A | Ldh_1_N | e5ldhA2 | A: a/b three-layered sandwiches | X: Rossmann-like | H: Rossmann-related | T: NAD(P)-binding Rossmann-fold domains | F: Ldh_1_N | ECOD (1.6) |
Domain Annotation: CATH CATH Database Homepage
Chain | Domain | Class | Architecture | Topology | Homology | Provenance Source (Version) |
---|---|---|---|---|---|---|
B | 3.40.50.720 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | NAD(P)-binding Rossmann-like Domain | CATH (4.3.0) |
B | 3.90.110.10 | Alpha Beta | Alpha-Beta Complex | L-2-Hydroxyisocaproate Dehydrogenase | Chain A, domain 2 | CATH (4.3.0) |
A | 3.40.50.720 | Alpha Beta | 3-Layer(aba) Sandwich | Rossmann fold | NAD(P)-binding Rossmann-like Domain | CATH (4.3.0) |
A | 3.90.110.10 | Alpha Beta | Alpha-Beta Complex | L-2-Hydroxyisocaproate Dehydrogenase | Chain A, domain 2 | CATH (4.3.0) |
Protein Family Annotation Pfam Database Homepage
Chains | Accession | Name | Description | Comments | Source |
---|---|---|---|---|---|
PF02866 | lactate/malate dehydrogenase, alpha/beta C-terminal domain (Ldh_1_C) | lactate/malate dehydrogenase, alpha/beta C-terminal domain | L-lactate dehydrogenases are metabolic enzymes which catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyse the in ... | Domain | |
PF00056 | lactate/malate dehydrogenase, NAD binding domain (Ldh_1_N) | lactate/malate dehydrogenase, NAD binding domain | L-lactate dehydrogenases are metabolic enzymes which catalyse the conversion of L-lactate to pyruvate, the last step in anaerobic glycolysis. L-2-hydroxyisocaproate dehydrogenases are also members of the family. Malate dehydrogenases catalyse the in ... | Domain |
Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage
InterPro: Protein Family Classification InterPro Database Homepage
Chains | Accession | Name | Type |
---|---|---|---|
IPR011304 | L-lactate dehydrogenase | Family | |
IPR018177 | L-lactate dehydrogenase, active site | Active Site | |
IPR001236 | Lactate/malate dehydrogenase, N-terminal | Domain | |
IPR036291 | NAD(P)-binding domain superfamily | Homologous Superfamily | |
IPR015955 | Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal | Homologous Superfamily | |
IPR022383 | Lactate/malate dehydrogenase, C-terminal | Domain | |
IPR001557 | L-lactate/malate dehydrogenase | Family |
Protein Modification Annotation
Modified Residue(s) | ||
---|---|---|
Chain | Residue(s) | Description |
ACE | AA0041 , AA0042 , AA0043 , AA0044 , AA0045 , AA0046 , AA0049 , AA0050 , AA0051 , AA0052 , AA0053 , AA0054 , AA0354 :  N-acetyl-L-alanine MOD:00050 , N-acetyl-L-aspartic acid MOD:00051 , N-acetyl-L-cysteine MOD:00052 , N-acetyl-S-archeol-cysteine MOD:00897 , N-acetyl-L-glutamic acid MOD:00053 , N-acetyl-L-glutamine MOD:00054 , N-acetylglycine MOD:00055 , N-acetyl-L-methionine MOD:00058 , N-acetyl-L-proline MOD:00059 , N-acetyl-L-serine MOD:00060 , N,O-diacetylated L-serine MOD:00648 , N-acetyl-L-threonine MOD:00061 , N-acetyl-L-tyrosine MOD:00062 , N-acetyl-L-valine MOD:00063 , N2-acetyl-L-arginine MOD:00359 | :