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2EI2

Crystal Structure Analysis of the 1,2-dihydroxynaphthalene dioxygenase from Pseudomonas sp. stain C18

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0006725biological_processobsolete cellular aromatic compound metabolic process
A0008198molecular_functionferrous iron binding
A0016702molecular_functionoxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
A0018554molecular_function1,2-dihydroxynaphthalene dioxygenase activity
A0019439biological_processobsolete aromatic compound catabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A1901170biological_processnaphthalene catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE MG A 398
ChainResidue
AGLU177
AHOH905
AHOH906
AHOH907
AHOH908
AHOH932

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FE2 A 399
ChainResidue
AGLU266
AHOH903
AHOH904
AHIS152
AHIS215
ATYR256

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 901
ChainResidue
ATYR12
ATRP51
AHIS52
AHIS53
AARG103
AMET104
APRO125
AARG126

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE GOL A 902
ChainResidue
APHE192
AHIS247
ATYR256
ALEU297
AHOH904
AHOH1143

Functional Information from PROSITE/UniProt
site_idPS00082
Number of Residues22
DetailsEXTRADIOL_DIOXYGENAS Extradiol ring-cleavage dioxygenases signature. GiHandkaltFYgaTPsGwliE
ChainResidueDetails
AGLY245-GLU266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING:
ChainResidueDetails
AHIS152
AASP199
AHIS215
ATYR256
AGLU266

Catalytic Information from CSA
site_idCSA1
Number of Residues3
DetailsAnnotated By Reference To The Literature 1mpy
ChainResidueDetails
AHIS200
ATYR256
AHIS247

219140

PDB entries from 2024-05-01

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