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1IAY

CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH COFACTOR PLP AND INHIBITOR AVG

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0009058biological_processbiosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLP A 500
ChainResidue
AGLY126
ASER277
ALYS278
AARG286
AALA127
ATHR128
ATYR152
AASN209
AASP237
AILE239
ATYR240
ASER275

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE AVG A 501
ChainResidue
ALEU53
AALA54
ATYR152
AALA154
ALYS278
AARG412
AHOH503

Functional Information from PROSITE/UniProt
site_idPS00105
Number of Residues14
DetailsAA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLSKdmGLpGFRVG
ChainResidueDetails
ASER275-GLY288

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING:
ChainResidueDetails
AGLU55
ATYR92

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS278

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ATYR152
AASP237

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
ALYS278
ATYR152
AASP237

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP91

237735

PDB entries from 2025-06-18

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