Loading
PDBj
English日本語简体中文繁體中文한국어
✖
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help
SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

1NDO

NAPHTHALENE 1,2-DIOXYGENASE

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0016491molecular_functionoxidoreductase activity
A0018625molecular_functionnaphthalene 1,2-dioxygenase activity
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0005515molecular_functionprotein binding
B0016491molecular_functionoxidoreductase activity
B0019380biological_process3-phenylpropionate catabolic process
B0051213molecular_functiondioxygenase activity
C0005506molecular_functioniron ion binding
C0005515molecular_functionprotein binding
C0016491molecular_functionoxidoreductase activity
C0018625molecular_functionnaphthalene 1,2-dioxygenase activity
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
C0051536molecular_functioniron-sulfur cluster binding
C0051537molecular_function2 iron, 2 sulfur cluster binding
D0005515molecular_functionprotein binding
D0016491molecular_functionoxidoreductase activity
D0019380biological_process3-phenylpropionate catabolic process
D0051213molecular_functiondioxygenase activity
E0005506molecular_functioniron ion binding
E0005515molecular_functionprotein binding
E0016491molecular_functionoxidoreductase activity
E0018625molecular_functionnaphthalene 1,2-dioxygenase activity
E0046872molecular_functionmetal ion binding
E0051213molecular_functiondioxygenase activity
E0051536molecular_functioniron-sulfur cluster binding
E0051537molecular_function2 iron, 2 sulfur cluster binding
F0005515molecular_functionprotein binding
F0016491molecular_functionoxidoreductase activity
F0019380biological_process3-phenylpropionate catabolic process
F0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE A 452
ChainResidue
AHIS208
AHIS213
AASP362
site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE C 452
ChainResidue
CASN201
CHIS208
CHIS213
CASP362
site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE FE E 452
ChainResidue
EHIS208
EHIS213
EASP362
site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES A 451
ChainResidue
ACYS81
AHIS83
AARG84
ACYS101
ATYR103
AHIS104
ATRP106
site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES C 451
ChainResidue
CCYS81
CHIS83
CARG84
CCYS101
CTYR103
CHIS104
CTRP106
site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE FES E 451
ChainResidue
ECYS81
EHIS83
EARG84
ECYS101
ETYR103
EHIS104
ETRP106
site_idMO1
Number of Residues3
DetailsMONO IRON SITE - THERE IS ALSO A WATER.
ChainResidue
AHIS213
AHIS208
AASP362
site_idMO2
Number of Residues3
DetailsMONO IRON SITE - THERE IS ALSO A WATER.
ChainResidue
CASP362
CHIS213
CHIS208
site_idMO3
Number of Residues3
DetailsMONO IRON SITE - THERE IS ALSO A WATER.
ChainResidue
EHIS213
EHIS208
EASP362
site_idRK1
Number of Residues4
DetailsRIESKE CENTER - FIRST TWO ARE LIGANDS TO FE1 AND THE NEXT TO FE2.
ChainResidue
ACYS81
ACYS101
AHIS83
CHIS104
site_idRK2
Number of Residues4
DetailsRIESKE CENTER - FIRST TWO ARE LIGANDS TO FE1 AND THE NEXT TO FE2.
ChainResidue
CCYS81
CCYS101
CHIS83
CHIS104
site_idRK3
Number of Residues4
DetailsRIESKE CENTER - FIRST TWO ARE LIGANDS TO FE1 AND THE NEXT TO FE2.
ChainResidue
ECYS81
ECYS101
EHIS83
EHIS104
Functional Information from PROSITE/UniProt
site_idPS00570
Number of Residues24
DetailsRING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGktlvsveaGNakgfvCsYH
ChainResidueDetails
ACYS81-HIS104
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues294
DetailsDomain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues18
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10669618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12586937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15942729","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9634695","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EG9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NDO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UUV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UUW","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10669618","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12586937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15942729","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9634695","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1EG9","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1NDO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7H","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7M","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7N","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7P","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1O7W","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1UUV","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues3
DetailsSite: {"description":"Important for enantioselectivity","evidences":[{"source":"PubMed","id":"10692370","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
Catalytic Information from CSA
site_idCSA1
Number of Residues3
Details
ChainResidueDetails
AHIS208
AASP205
CHIS104
site_idCSA2
Number of Residues3
Details
ChainResidueDetails
AHIS104
EHIS208
EASP205
site_idCSA3
Number of Residues3
Details
ChainResidueDetails
CHIS208
CASP205
EHIS104
site_idMCSA1
Number of Residues5
DetailsM-CSA 130
ChainResidueDetails
AHIS104single electron acceptor, single electron donor, single electron relay
AASP205single electron acceptor, single electron donor, single electron relay
AHIS208metal ligand, single electron acceptor, single electron donor, single electron relay
AHIS213metal ligand
AASP362metal ligand
site_idMCSA2
Number of Residues5
DetailsM-CSA 130
ChainResidueDetails
CHIS104single electron acceptor, single electron donor, single electron relay
CASP205single electron acceptor, single electron donor, single electron relay
CHIS208metal ligand, single electron acceptor, single electron donor, single electron relay
CHIS213metal ligand
CASP362metal ligand
site_idMCSA3
Number of Residues5
DetailsM-CSA 130
ChainResidueDetails
EHIS104single electron acceptor, single electron donor, single electron relay
EASP205single electron acceptor, single electron donor, single electron relay
EHIS208metal ligand, single electron acceptor, single electron donor, single electron relay
EHIS213metal ligand
EASP362metal ligand

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon