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5TF5

CRYSTAL STRUCTURE OF HUMAN KAT-2 IN COMPLEX WITH A REVERSIBLE INHIBITOR

Functional Information from GO Data
ChainGOidnamespacecontents
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0006103biological_process2-oxoglutarate metabolic process
A0006536biological_processglutamate metabolic process
A0008483molecular_functiontransaminase activity
A0009058biological_processbiosynthetic process
A0016212molecular_functionkynurenine-oxoglutarate transaminase activity
A0016740molecular_functiontransferase activity
A0030170molecular_functionpyridoxal phosphate binding
A0033512biological_processL-lysine catabolic process to acetyl-CoA via saccharopine
A0042803molecular_functionprotein homodimerization activity
A0047315molecular_functionkynurenine-glyoxylate transaminase activity
A0047536molecular_function2-aminoadipate transaminase activity
A0047958molecular_functionglycine:2-oxoglutarate aminotransferase activity
A0050094molecular_functionmethionine-glyoxylate transaminase activity
A0070189biological_processkynurenine metabolic process
A1901605biological_processalpha-amino acid metabolic process
B0005739cellular_componentmitochondrion
B0005759cellular_componentmitochondrial matrix
B0006103biological_process2-oxoglutarate metabolic process
B0006536biological_processglutamate metabolic process
B0008483molecular_functiontransaminase activity
B0009058biological_processbiosynthetic process
B0016212molecular_functionkynurenine-oxoglutarate transaminase activity
B0016740molecular_functiontransferase activity
B0030170molecular_functionpyridoxal phosphate binding
B0033512biological_processL-lysine catabolic process to acetyl-CoA via saccharopine
B0042803molecular_functionprotein homodimerization activity
B0047315molecular_functionkynurenine-glyoxylate transaminase activity
B0047536molecular_function2-aminoadipate transaminase activity
B0047958molecular_functionglycine:2-oxoglutarate aminotransferase activity
B0050094molecular_functionmethionine-glyoxylate transaminase activity
B0070189biological_processkynurenine metabolic process
B1901605biological_processalpha-amino acid metabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue 7AR B 501
ChainResidue
AILE19
BASN202
BTYR233
BLLP263
BMET354
BPHE355
BLEU382
BPHE387
BARG399
AMET22
AGLY39
APRO41
ATYR74
AHOH783
BGLN118
BTYR142
BSER143

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues56
DetailsTransit peptide: {"description":"Mitochondrion","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues54
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues20
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues10
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9WVM8","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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