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1UW8

CRYSTAL STRUCTURE OF OXALATE DECARBOXYLASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
A0016829molecular_functionlyase activity
A0016831molecular_functioncarboxy-lyase activity
A0033609biological_processoxalate metabolic process
A0046564molecular_functionoxalate decarboxylase activity
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A1383
ChainResidue
AHIS95
AHIS97
AGLU101
AHIS140
AHOH2397
AHOH2398

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A1384
ChainResidue
AHIS319
AGLU333
AHOH2399
AHIS273
AHIS275
AGLU280

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS A1385
ChainResidue
AGLU117
APRO135
ASER136
AASN277
AHIS339
AALA341
AHOH2400
AHOH2401
AHOH2402

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues142
DetailsDomain: {"description":"Cupin type-1 1","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues141
DetailsDomain: {"description":"Cupin type-1 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues23
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12056897","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12056897","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
Details
ChainResidueDetails
AARG92
AGLU162

site_idMCSA1
Number of Residues6
DetailsM-CSA 231
ChainResidueDetails
AARG92attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
AHIS95metal ligand
AHIS97metal ligand
AGLU101metal ligand
AHIS140metal ligand
AGLU162electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2025-07-09

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