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5HI0

The Substrate Binding Mode and Chemical Basis of a Reaction Specificity Switch in Oxalate Decarboxylase

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 CO A 401
ChainResidue
AHIS95
AHIS97
AGLU101
AHIS140
AOXL403
AHOH516

site_idAC2
Number of Residues7
Detailsbinding site for residue CO A 402
ChainResidue
AHIS318
AGLU332
AHOH503
AHOH524
AHIS272
AHIS274
AGLU279

site_idAC3
Number of Residues11
Detailsbinding site for residue OXL A 403
ChainResidue
AMET84
AARG92
AHIS95
AHIS97
AGLU101
AHIS140
ALEU153
ATHR164
ACO401
AHOH513
AHOH516

site_idAC4
Number of Residues1
Detailsbinding site for residue NA A 404
ChainResidue
AHOH543

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsACT_SITE: Proton donor => ECO:0000269|PubMed:12056897
ChainResidueDetails
AILE333

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:12056897
ChainResidueDetails
AHIS95
AHIS97
AGLU101
AHIS140
ATRP273
APRO275
ATRP280
ATYR319

Catalytic Information from CSA
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
AASN162electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor

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PDB entries from 2024-07-17

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