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1L3J

Crystal Structure of Oxalate Decarboxylase Formate Complex

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 Residues5
DetailsBINDING SITE FOR RESIDUE MN A 500
ChainResidue
AHIS95
AHIS97
AGLU101
AHIS140
AFMT550

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MN A 501
ChainResidue
AGLU333
AHOH891
AHOH895
AHIS273
AHIS275
AGLU280
AHIS319

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE MG A 502
ChainResidue
AHIS174
AFMT650
AHOH1033
AHOH1034

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE FMT A 550
ChainResidue
AMET84
AARG92
AHIS95
AHIS97
AGLU101
ALEU153
APHE155
AMN500
AHOH976

site_idAC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE FMT A 650
ChainResidue
AGLU39
AMG502

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
AGLU162electrostatic 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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