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2V09

SENS161-164DSSN mutant of Bacillus subtilis Oxalate Decarboxylase OxdC

Functional Information from GO Data
ChainGOidnamespacecontents
A0005737cellular_componentcytoplasm
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
AHOH2466
AHOH2467

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MN A1384
ChainResidue
AHIS319
AGLU333
AHOH2468
AHIS273
AHIS275
AGLU280

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE TRS A1385
ChainResidue
AGLU117
APRO135
ASER136
APRO276
AASN277
AHIS339
AALA341
AHOH2469
AHOH2470
AHOH2471

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:12056897
ChainResidueDetails
AGLU333

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12056897
ChainResidueDetails
AHIS95
AHIS97
AGLU101
AHIS140
AHIS273
AHIS275
AGLU280
AHIS319

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 Residues6
DetailsM-CSA 231
ChainResidueDetails
AARG92attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor
AHIS95metal ligand
AHIS97metal ligand
AGLU101metal ligand
AHIS140metal ligand
ASER162electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-07-24

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