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5G2P

The crystal structure of a S-selective transaminase from Arthrobacter sp.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005829cellular_componentcytosol
A0008483molecular_functiontransaminase activity
A0030170molecular_functionpyridoxal phosphate binding
B0005829cellular_componentcytosol
B0008483molecular_functiontransaminase activity
B0030170molecular_functionpyridoxal phosphate binding
C0005829cellular_componentcytosol
C0008483molecular_functiontransaminase activity
C0030170molecular_functionpyridoxal phosphate binding
D0005829cellular_componentcytosol
D0008483molecular_functiontransaminase activity
D0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP A 2000
ChainResidue
AGLY121
ALYS298
AHOH3149
AHOH3172
AHOH3174
AHOH3264
AHOH3266
BTHR330
ASER122
ATYR148
AHIS149
AGLY150
AGLU237
AASP269
AVAL271
ALEU272

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP B 2000
ChainResidue
ATHR330
AHOH3150
AHOH3284
AHOH3285
AHOH3287
BGLY121
BSER122
BTYR148
BHIS149
BGLY150
BGLU237
BASP269
BVAL271
BLEU272
BLYS298
BHOH3206

site_idAC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP C 2000
ChainResidue
CGLY121
CSER122
CTYR148
CHIS149
CGLU237
CASP269
CVAL271
CLEU272
CLYS298
CHOH3114
CHOH3137
CHOH3171
CHOH3198
CHOH3199
DTHR330

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP D 2000
ChainResidue
CTHR330
CHOH3115
CHOH3218
CHOH3219
CHOH3221
DGLY121
DSER122
DTYR148
DHIS149
DGLY150
DGLU237
DASP269
DVAL271
DLEU272
DLYS298
DHOH3134

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL C 1474
ChainResidue
CARG144
CSER195
CHOH3175

site_idAC6
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL B 1474
ChainResidue
BARG144
BSER195
BHOH3132

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL D 1474
ChainResidue
DARG144
DSER195

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1475
ChainResidue
AARG144
ASER195

Functional Information from PROSITE/UniProt
site_idPS00599
Number of Residues10
DetailsAA_TRANSFER_CLASS_2 Aminotransferases class-II pyridoxal-phosphate attachment site. TMGKGLSSSS
ChainResidueDetails
ATHR295-SER304

site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. WIsDEVlt.GFgRtGkwfgyqhygvqp....DIItmGKglsSS
ChainResidueDetails
ATRP266-SER303

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PDB entries from 2025-06-18

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