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5VWO

Ornithine aminotransferase inactivated by (1R,3S,4S)-3-amino-4-fluorocyclopentane-1-carboxylic acid (FCP)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004587molecular_functionornithine aminotransferase activity
A0005515molecular_functionprotein binding
A0005654cellular_componentnucleoplasm
A0005737cellular_componentcytoplasm
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0007601biological_processvisual perception
A0008483molecular_functiontransaminase activity
A0010121biological_processarginine catabolic process to proline via ornithine
A0019544biological_processarginine catabolic process to glutamate
A0030170molecular_functionpyridoxal phosphate binding
A0042802molecular_functionidentical protein binding
A0055129biological_processL-proline biosynthetic process
B0004587molecular_functionornithine aminotransferase activity
B0005515molecular_functionprotein binding
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0007601biological_processvisual perception
B0008483molecular_functiontransaminase activity
B0010121biological_processarginine catabolic process to proline via ornithine
B0019544biological_processarginine catabolic process to glutamate
B0030170molecular_functionpyridoxal phosphate binding
B0042802molecular_functionidentical protein binding
B0055129biological_processL-proline biosynthetic process
C0004587molecular_functionornithine aminotransferase activity
C0005515molecular_functionprotein binding
C0005654cellular_componentnucleoplasm
C0005737cellular_componentcytoplasm
C0005739cellular_componentmitochondrion
C0005759cellular_componentmitochondrial matrix
C0007601biological_processvisual perception
C0008483molecular_functiontransaminase activity
C0010121biological_processarginine catabolic process to proline via ornithine
C0019544biological_processarginine catabolic process to glutamate
C0030170molecular_functionpyridoxal phosphate binding
C0042802molecular_functionidentical protein binding
C0055129biological_processL-proline biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues19
Detailsbinding site for residue 9QJ A 500
ChainResidue
ATYR85
AILE265
AGLN266
ALYS292
AHOH627
AHOH663
AHOH688
AHOH752
AHOH772
AHOH792
BTHR322
AGLY142
AVAL143
APHE177
ATRP178
AGLY179
AARG180
AGLU235
AASP263

site_idAC2
Number of Residues24
Detailsbinding site for Di-peptide 9QJ B 500 and LYS B 292
ChainResidue
ATHR322
ATYR323
BTYR85
BGLY142
BVAL143
BPHE177
BTRP178
BGLY179
BARG180
BGLU235
BASP263
BILE265
BGLN266
BGLY291
BALA293
BLEU294
BSER295
BHOH647
BHOH664
BHOH698
BHOH739
BHOH806
BHOH807
BHOH828

site_idAC3
Number of Residues27
Detailsbinding site for Di-peptide 9QJ C 500 and LYS C 292
ChainResidue
CTYR85
CALA87
CGLY142
CVAL143
CPHE177
CTRP178
CGLY179
CARG180
CGLU235
CASP263
CILE265
CGLN266
CGLY291
CALA293
CLEU294
CSER295
CTHR322
CTYR323
CHOH612
CHOH670
CHOH674
CHOH686
CHOH743
CHOH747
CHOH790
CHOH801
CHOH848

Functional Information from PROSITE/UniProt
site_idPS00600
Number of Residues38
DetailsAA_TRANSFER_CLASS_3 Aminotransferases class-III pyridoxal-phosphate attachment site. FIaDEIqt.GLaRtGrwlavdyenvrp....DIVllGKalsGG
ChainResidueDetails
APHE260-GLY297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues15
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P29758
ChainResidueDetails
ALYS49
BLYS421
CLYS49
CLYS66
CLYS386
CLYS392
CLYS421
ALYS66
ALYS386
ALYS392
ALYS421
BLYS49
BLYS66
BLYS386
BLYS392

site_idSWS_FT_FI2
Number of Residues3
DetailsMOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P29758
ChainResidueDetails
ALYS102
BLYS102
CLYS102

site_idSWS_FT_FI3
Number of Residues9
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P29758
ChainResidueDetails
ALYS107
ALYS362
ALYS405
BLYS107
BLYS362
BLYS405
CLYS107
CLYS362
CLYS405

site_idSWS_FT_FI4
Number of Residues3
DetailsMOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:3754226
ChainResidueDetails
ALYS292
BLYS292
CLYS292

Catalytic Information from CSA
site_idMCSA1
Number of Residues3
DetailsM-CSA 929
ChainResidueDetails
APHE177steric role
AASP263electrostatic stabiliser
ALYS292covalent catalysis, proton shuttle (general acid/base)

site_idMCSA2
Number of Residues3
DetailsM-CSA 929
ChainResidueDetails
BPHE177steric role
BASP263electrostatic stabiliser
BLYS292covalent catalysis, proton shuttle (general acid/base)

site_idMCSA3
Number of Residues3
DetailsM-CSA 929
ChainResidueDetails
CPHE177steric role
CASP263electrostatic stabiliser
CLYS292covalent catalysis, proton shuttle (general acid/base)

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PDB entries from 2024-07-24

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