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6F2E

Crystal structure of the APO Fe(II)/alpha-ketoglutarate dependent dioxygenase KDO1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0016491molecular_functionoxidoreductase activity
A0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
A0055114biological_processobsolete oxidation-reduction process
B0005506molecular_functioniron ion binding
B0016491molecular_functionoxidoreductase activity
B0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
B0055114biological_processobsolete oxidation-reduction process
C0005506molecular_functioniron ion binding
C0016491molecular_functionoxidoreductase activity
C0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
C0055114biological_processobsolete oxidation-reduction process
D0005506molecular_functioniron ion binding
D0016491molecular_functionoxidoreductase activity
D0016706molecular_function2-oxoglutarate-dependent dioxygenase activity
D0055114biological_processobsolete oxidation-reduction process
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue ACY A 401
ChainResidue
AMET156
ATHR204
AARG316
AARG328
AHOH526

site_idAC2
Number of Residues6
Detailsbinding site for residue ACY B 401
ChainResidue
BLEU330
BHOH633
BTHR204
BHIS314
BARG316
BARG328

site_idAC3
Number of Residues6
Detailsbinding site for residue ACY C 401
ChainResidue
CMET156
CTHR204
CARG316
CARG328
CHOH509
CHOH622

site_idAC4
Number of Residues5
Detailsbinding site for residue ACY D 401
ChainResidue
DTHR204
DHIS314
DARG316
DARG328
DHOH544

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9Z4Z5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

253091

PDB entries from 2026-05-06

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