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1DLQ

STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 INHIBITED BY BOUND MERCURY

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0008199molecular_functionferric iron binding
A0009712biological_processcatechol-containing compound metabolic process
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0018576molecular_functioncatechol 1,2-dioxygenase activity
A0019614biological_processcatechol-containing compound catabolic process
A0042952biological_processbeta-ketoadipate pathway
B0003824molecular_functioncatalytic activity
B0005506molecular_functioniron ion binding
B0008199molecular_functionferric iron binding
B0009712biological_processcatechol-containing compound metabolic process
B0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
B0018576molecular_functioncatechol 1,2-dioxygenase activity
B0019614biological_processcatechol-containing compound catabolic process
B0042952biological_processbeta-ketoadipate pathway
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE A 400
ChainResidue
ATYR164
ATYR200
AARG221
AHIS224
AHIS226
AHOH501

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG A 401
ChainResidue
APHE253
AHOH505
AGLY201
ACYS202
AGLY219

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE HG A 402
ChainResidue
AGLY201
ACYS202
AGLN209

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG A 403
ChainResidue
AHIS82
AMET86

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE B 400
ChainResidue
BTYR164
BTYR200
BARG221
BHIS224
BHIS226
BHOH503

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE HG B 401
ChainResidue
BGLY201
BCYS202
BGLY219
BPHE253
BHOH513

site_idAC7
Number of Residues4
DetailsBINDING SITE FOR RESIDUE HG B 402
ChainResidue
BGLY201
BCYS202
BGLN209
BGLY219

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE HG B 403
ChainResidue
BHIS82
BMET86

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE LIO B 999
ChainResidue
AASN27
APHE80
BGLU54
BTYR61
BLEU62
BGLN210

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LIO A 1999
ChainResidue
AGLU54
ATYR55
ATYR61
AGLN214

Functional Information from PROSITE/UniProt
site_idPS00083
Number of Residues29
DetailsINTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. LhGtIfdadGkpLpnakVEIwhantkGfY
ChainResidueDetails
ALEU136-TYR164

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10801478","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DLM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DLQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DLT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DMH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10801478","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DLM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1DLQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10801478","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1DLT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 3pca
ChainResidueDetails
AARG221
ATYR200

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 3pca
ChainResidueDetails
BARG221
BTYR200

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PDB entries from 2026-03-25

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