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1IAX

CRYSTAL STRUCTURE OF ACC SYNTHASE COMPLEXED WITH PLP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0009058biological_processbiosynthetic process
A0030170molecular_functionpyridoxal phosphate binding
B0003824molecular_functioncatalytic activity
B0009058biological_processbiosynthetic process
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 600
ChainResidue
AALA54
ATYR152
AASN209
ATYR240
AARG412

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 601
ChainResidue
BPLP501
BLEU53
BALA54
BTYR152
BARG412

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE PLP A 500
ChainResidue
AGLY126
AALA127
ATHR128
ATYR152
AASN209
AILE239
ATYR240
ASER275
ASER277
ALYS278
AARG286

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR RESIDUE PLP B 501
ChainResidue
BGLY126
BALA127
BTHR128
BTYR152
BASN209
BILE239
BTYR240
BSER275
BSER277
BLYS278
BARG286
BSO4601

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 Residues4
DetailsBINDING:
ChainResidueDetails
AGLU55
ATYR92
BGLU55
BTYR92

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine
ChainResidueDetails
ALYS278
BLYS278

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PDB entries from 2024-06-12

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