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1DMH

STRUCTURE OF CATECHOL 1,2-DIOXYGENASE FROM ACINETOBACTER SP. ADP1 WITH BOUND 4-METHYLCATECHOL

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
A0005575cellular_componentcellular_component
A0008199molecular_functionferric iron binding
A0009056biological_processcatabolic process
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
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
B0003824molecular_functioncatalytic activity
B0005506molecular_functioniron ion binding
B0005575cellular_componentcellular_component
B0008199molecular_functionferric iron binding
B0009056biological_processcatabolic process
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
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 400
ChainResidue
ATYR164
AHIS224
AHIS226
AMCT401
AHOH501

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE B 400
ChainResidue
BHOH503
BTYR164
BHIS224
BHIS226
BMCT401

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MCT A 401
ChainResidue
ALEU73
APRO76
APRO108
ALEU109
ATYR164
ATYR200
AARG221
AHIS224
AHIS226
AFE400
AHOH501

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LIO B 999
ChainResidue
BGLU54
BTYR61
BLEU62
BHOH745

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE MCT B 401
ChainResidue
BLEU73
BPRO76
BGLY107
BPRO108
BTYR164
BTYR200
BARG221
BHIS224
BHIS226
BFE400
BHOH503

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE LIO A 1999
ChainResidue
AGLU54
ATYR61
ALEU62
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: BINDING => ECO:0000269|PubMed:10801478, ECO:0007744|PDB:1DLM, ECO:0007744|PDB:1DLQ, ECO:0007744|PDB:1DLT, ECO:0007744|PDB:1DMH
ChainResidueDetails
ATYR164
AHIS224
AHIS226
BTYR164
BHIS224
BHIS226

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:10801478, ECO:0007744|PDB:1DLM, ECO:0007744|PDB:1DLQ
ChainResidueDetails
ATYR200
BTYR200

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 2024-07-10

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