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2XH1

Crystal structure of human KAT II-inhibitor complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016212molecular_functionL-kynurenine:2-oxoglutarate transaminase activity
A0019477biological_processL-lysine catabolic process
A0030170molecular_functionpyridoxal phosphate binding
A0047313molecular_functionaromatic-amino-acid:glyoxylate transaminase activity
A0047315molecular_functionL-kynurenine:glyoxylate transaminase activity
A0047536molecular_functionL-2-aminoadipate:2-oxoglutarate transaminase activity
A0047958molecular_functionglycine:2-oxoglutarate transaminase activity
A0050094molecular_functionL-methionine:glyoxylate transaminase activity
A1901605biological_processalpha-amino acid metabolic process
A1901606biological_processalpha-amino acid catabolic process
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0016212molecular_functionL-kynurenine:2-oxoglutarate transaminase activity
B0019477biological_processL-lysine catabolic process
B0030170molecular_functionpyridoxal phosphate binding
B0047313molecular_functionaromatic-amino-acid:glyoxylate transaminase activity
B0047315molecular_functionL-kynurenine:glyoxylate transaminase activity
B0047536molecular_functionL-2-aminoadipate:2-oxoglutarate transaminase activity
B0047958molecular_functionglycine:2-oxoglutarate transaminase activity
B0050094molecular_functionL-methionine:glyoxylate transaminase activity
B1901605biological_processalpha-amino acid metabolic process
B1901606biological_processalpha-amino acid catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE BF5 A 1426
ChainResidue
ATYR142
APLP1427
AHOH2240
AHOH2241
BGLY39
BLEU40
BSER75
BPRO76

site_idAC2
Number of Residues14
DetailsBINDING SITE FOR RESIDUE PLP A 1427
ChainResidue
AGLN118
ATYR142
AASN202
AASP230
APRO232
ATYR233
ASER260
ASER262
ALYS263
AARG270
ABF51426
AHOH2187
BTYR74
ASER117

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BF5 B 1426
ChainResidue
AGLY39
ALEU40
ATYR74
ASER77
BTYR142
BPLP1427

site_idAC4
Number of Residues13
DetailsBINDING SITE FOR RESIDUE PLP B 1427
ChainResidue
ATYR74
BSER117
BGLN118
BTYR142
BASN202
BASP230
BPRO232
BTYR233
BSER260
BSER262
BLYS263
BARG270
BBF51426

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE IOD A 1428
ChainResidue
AGLN119
ALYS123
BGLN119
BLYS123

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 1428
ChainResidue
BGLU-1
BASN2
BSER105
BPRO279
BHOH2173
BHOH2174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues54
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues20
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues8
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

253091

PDB entries from 2026-05-06

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