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1O4T

Crystal structure of a predicted oxalate decarboxylase (tm1287) from thermotoga maritima at 1.95 A resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0030145molecular_functionmanganese ion binding
A0033609biological_processoxalate metabolic process
A0042802molecular_functionidentical protein binding
A0042803molecular_functionprotein homodimerization activity
A0046564molecular_functionoxalate decarboxylase activity
A0046872molecular_functionmetal ion binding
B0030145molecular_functionmanganese ion binding
B0033609biological_processoxalate metabolic process
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0046564molecular_functionoxalate decarboxylase activity
B0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN A 300
ChainResidue
AHIS61
AHIS63
AGLU68
AHIS102
AOXL400

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MN B 301
ChainResidue
BOXL401
BHIS61
BHIS63
BGLU68
BHIS102

site_idAC3
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OXL A 400
ChainResidue
AHIS61
AHIS63
AGLU68
ATYR70
AHIS102
AMN300
AHOH491

site_idAC4
Number of Residues9
DetailsBINDING SITE FOR RESIDUE OXL B 401
ChainResidue
BARG23
BHIS61
BHIS63
BGLU68
BTYR70
BHIS102
BILE118
BMN301
BHOH506

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:15211523, ECO:0007744|PDB:1O4T
ChainResidueDetails
AHIS61
AHIS63
AGLU68
AHIS102
BHIS61
BHIS63
BGLU68
BHIS102

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:15211523
ChainResidueDetails
ATYR70
BTYR70

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1gqg
ChainResidueDetails
AGLU68

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1gqg
ChainResidueDetails
BGLU68

219140

PDB entries from 2024-05-01

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