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2E54

Crystal structure of acetylornithine aminotransferase from Thermotoga maritima

Functional Information from GO Data
ChainGOidnamespacecontents
A0003992molecular_functionN2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity
A0005737cellular_componentcytoplasm
A0006525biological_processarginine metabolic process
A0006526biological_processarginine biosynthetic process
A0008483molecular_functiontransaminase activity
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 1004
ChainResidue
ALYS310
ATYR313
AVAL316
ANA1005
AHOH1043
AHOH1071
AHOH1073

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NA A 1005
ChainResidue
AHOH1071
AHOH1073
AHOH1203
AHOH1392
AHOH1474
ANA1004
AHOH1043

site_idAC3
Number of Residues18
DetailsBINDING SITE FOR RESIDUE PLP A 1001
ChainResidue
ATHR93
AGLY94
ATHR95
APHE126
AHIS127
AGLU178
AGLU183
AASP211
AVAL213
AGLN214
ALYS240
ATHR268
AHOH1024
AHOH1029
AHOH1030
AHOH1037
AHOH1040
AHOH1075

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1002
ChainResidue
AGLU294
ALYS298
ALEU364
ATHR365
AHOH1173
AHOH1336

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1003
ChainResidue
AASP32
ASER35
AASN40
AHIS44
APRO363

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. LVfDEVqc.GMgRtGklfayqkygvvp....DVLttAKglgGG
ChainResidueDetails
ALEU208-GLY245

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|Ref.2, ECO:0000269|Ref.3
ChainResidueDetails
AGLY94

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305|Ref.2, ECO:0000305|Ref.3
ChainResidueDetails
APHE126
AASP211

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107
ChainResidueDetails
ATHR267
AARG129

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|Ref.3
ChainResidueDetails
ATHR268

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000255|HAMAP-Rule:MF_01107
ChainResidueDetails
ALYS240

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PDB entries from 2024-06-12

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