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4AON

Conformational dynamics of aspartate alpha-decarboxylase active site revealed by protein-ligand complexes: 1-methyl-L-aspartate complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0004068molecular_functionaspartate 1-decarboxylase activity
A0006523biological_processalanine biosynthetic process
B0004068molecular_functionaspartate 1-decarboxylase activity
B0006523biological_processalanine biosynthetic process
D0004068molecular_functionaspartate 1-decarboxylase activity
D0006523biological_processalanine biosynthetic process
E0004068molecular_functionaspartate 1-decarboxylase activity
E0006523biological_processalanine biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU B 1123
ChainResidue
ATYR22
DHIS11
ETRP47
EARG54
EILE86
AGLY24
BPYR25
BTHR57
BTYR58
BGLY73
BALA74
BALA75
DLYS9

site_idAC2
Number of Residues13
DetailsBINDING SITE FOR RESIDUE GLU E 1116
ChainResidue
ALYS9
AHIS11
BTRP47
BARG54
BILE86
DTYR22
EPYR25
ETHR57
ETYR58
EASN72
EGLY73
EALA74
EALA75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Schiff-base intermediate with substrate; via pyruvic acid => ECO:0000269|PubMed:9546220
ChainResidueDetails
EPYR25
BPYR25

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Proton donor
ChainResidueDetails
BTYR58
ETYR58

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ETHR57
EGLY73
BTHR57
BGLY73

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Pyruvic acid (Ser) => ECO:0000269|PubMed:9546220
ChainResidueDetails
EPYR25
BPYR25

Catalytic Information from CSA
site_idMCSA1
Number of Residues2
DetailsM-CSA 409
ChainResidueDetails
BPYR25covalently attached, electrofuge, electrophile
BTYR58activator, increase nucleophilicity, proton acceptor, proton donor

site_idMCSA2
Number of Residues2
DetailsM-CSA 409
ChainResidueDetails
EPYR25covalently attached, electrofuge, electrophile
ETYR58activator, increase nucleophilicity, proton acceptor, proton donor

221051

PDB entries from 2024-06-12

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