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2UYA

DEL162-163 mutant of Bacillus subtilis Oxalate Decarboxylase OxdC

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
AHOH2405
AHOH2406

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A1384
ChainResidue
AHIS319
AGLU333
AHOH2407
AHIS273
AHIS275
AGLU280

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE TRS A1385
ChainResidue
AGLU117
APRO135
ASER136
AASN277
AHIS339
AALA341
AHOH2408
AHOH2409
AHOH2410

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A1386
ChainResidue
AGLY43
AHIS56
AARG58
AHOH2411

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CL A1387
ChainResidue
AARG92
AHOH2149
AHOH2255
AHOH2406

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues141
DetailsDomain: {"description":"Cupin type-1 2","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues23
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsActive site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"12056897","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12056897","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1gqg
ChainResidueDetails
AGLU101

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1gqg
ChainResidueDetails
AGLU280

site_idMCSA1
Number of Residues5
DetailsM-CSA 231
ChainResidueDetails
AARG92attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
AHIS95metal ligand
AHIS97metal ligand
AGLU101metal ligand
AHIS140metal ligand

246704

PDB entries from 2025-12-24

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