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3TH1

Crystal structure of chlorocatechol 1,2-dioxygenase from Pseudomonas putida

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005506molecular_functioniron ion binding
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
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
B0003824molecular_functioncatalytic activity
B0005506molecular_functioniron ion binding
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
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
C0003824molecular_functioncatalytic activity
C0005506molecular_functioniron ion binding
C0008199molecular_functionferric iron binding
C0009056biological_processcatabolic process
C0009712biological_processcatechol-containing compound metabolic process
C0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
C0018576molecular_functioncatechol 1,2-dioxygenase activity
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE C 300
ChainResidue
CTYR130
CTYR164
CHIS188
CHIS190

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE B 300
ChainResidue
BTYR130
BTYR164
BHIS188
BHIS190

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE DTD B 301
ChainResidue
BPRO76
BTYR164
BARG185
BILE73

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 3PH B 302
ChainResidue
BGLU29
BALA32
BGLY33
BTYR36
BLEU37
BLEU50
BARG174
BHIS178
CVAL5
CVAL8

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL B 303
ChainResidue
BASP51
CTYR30
CVAL34
CASP35

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL B 306
ChainResidue
ALYS211
ATRP212
AASP215
BTRP212
BASP214
BASP215

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE A 300
ChainResidue
ATYR130
ATYR164
AHIS188
AHIS190
ADTD301

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE DTD A 301
ChainResidue
AASP51
AILE73
AGLY75
APRO76
ATYR164
AARG185
AFE300

site_idAC9
Number of Residues11
DetailsBINDING SITE FOR RESIDUE 3PH A 302
ChainResidue
AVAL5
AVAL8
AALA32
AGLY33
ATYR36
ALEU37
ALEU50
ALEU50
ALEU54
AARG174
AHIS178

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 303
ChainResidue
AARG103
AASN153

site_idBC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MG A 304
ChainResidue
ATHR239
AASP241

site_idBC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE ACT A 305
ChainResidue
ASER56
ATHR57
AGLU60
AHIS219

Functional Information from PROSITE/UniProt
site_idPS00083
Number of Residues29
DetailsINTRADIOL_DIOXYGENAS Intradiol ring-cleavage dioxygenases signature. IrGtVrsdtGelLagavIDVwhstpdGlY
ChainResidueDetails
AILE102-TYR130

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ATYR130
CTYR164
CHIS188
CHIS190
ATYR164
AHIS188
AHIS190
BTYR130
BTYR164
BHIS188
BHIS190
CTYR130

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PDB entries from 2024-10-30

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