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3S5O

Crystal Structure of Human 4-hydroxy-2-oxoglutarate Aldolase Bound to Pyruvate

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005739cellular_componentmitochondrion
A0005759cellular_componentmitochondrial matrix
A0008700molecular_function(R,S)-4-hydroxy-2-oxoglutarate aldolase activity
A0009436biological_processglyoxylate catabolic process
A0016829molecular_functionlyase activity
A0019470biological_processtrans-4-hydroxy-L-proline catabolic process
A0033609biological_processoxalate metabolic process
A0042803molecular_functionprotein homodimerization activity
A0042866biological_processpyruvate biosynthetic process
A0046487biological_processglyoxylate metabolic process
A0106009molecular_function(4S)-4-hydroxy-2-oxoglutarate aldolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1
ChainResidue
AGLU59
ALYS63
AHOH527
AHOH533

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 2
ChainResidue
AHOH527
ALYS63
APHE295
AGLY296
ATYR297
AHOH526

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 3
ChainResidue
AEDO6
ATYR141
AARG144
AGLY284
AILE285
APRO286
AHOH478
AHOH529

site_idAC4
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 4
ChainResidue
AVAL42
ATHR43
APRO45
ALEU57
AASN60
ALEU64
AASN244
AMET292

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 6
ChainResidue
AEDO3
ASER77
AASN173
AHOH341
AHOH537

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K A 328
ChainResidue
ASER187
AHIS189
AILE192
AASP216
AHOH342
AHOH371

Functional Information from PROSITE/UniProt
site_idPS00666
Number of Residues31
DetailsDHDPS_2 Dihydrodipicolinate synthase signature 2. YSVPanTgldLpvdavvtlsqhpn.IvGMKDS
ChainResidueDetails
ATYR168-SER198

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Schiff-base intermediate with substrate","evidences":[{"source":"PubMed","id":"21998747","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsSite: {"description":"Involved in proton transfer during cleavage"}
ChainResidueDetails

250359

PDB entries from 2026-03-11

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