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3I5T

CRYSTAL STRUCTURE OF AMINOTRANSFERASE PRK07036 FROM Rhodobacter sphaeroides KD131

Functional Information from GO Data
ChainGOidnamespacecontents
A0008483molecular_functiontransaminase activity
A0030170molecular_functionpyridoxal phosphate binding
B0008483molecular_functiontransaminase activity
B0030170molecular_functionpyridoxal phosphate binding
Functional Information from PDB Data
site_idAC1
Number of Residues15
DetailsBINDING SITE FOR RESIDUE PLP A 474
ChainResidue
AGLY120
AHOH481
AHOH524
AHOH538
AHOH630
BTYR324
BTHR325
ASER121
ATYR153
AHIS154
AGLU225
AASP258
AVAL260
AVAL261
ALYS288

site_idAC2
Number of Residues16
DetailsBINDING SITE FOR RESIDUE PLP B 474
ChainResidue
ATYR324
ATHR325
BGLY120
BSER121
BTYR153
BHIS154
BGLU225
BASP258
BVAL260
BVAL261
BLYS288
BHOH512
BHOH518
BHOH550
BHOH672
BHOH722

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues39
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. YIsDEVvt.GFgRcGewfasekvfgvvp...DIItfAKgvtSG
ChainResidueDetails
ATYR255-GLY293

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP258
ALYS288
ATYR153

site_idCSA2
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP258
BLYS288
BTYR153

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
AASP258
ATYR153

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ay4
ChainResidueDetails
BASP258
BTYR153

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PDB entries from 2024-07-24

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