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1EG9

NAPHTHALENE 1,2-DIOXYGENASE WITH INDOLE BOUND IN THE ACTIVE SITE.

Functional Information from GO Data
ChainGOidnamespacecontents
A0005506molecular_functioniron ion binding
A0005515molecular_functionprotein binding
A0016491molecular_functionoxidoreductase activity
A0018625molecular_functionnaphthalene 1,2-dioxygenase activity
A0019439biological_processobsolete aromatic compound catabolic process
A0044237biological_processcellular metabolic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051536molecular_functioniron-sulfur cluster binding
A0051537molecular_function2 iron, 2 sulfur cluster binding
B0005515molecular_functionprotein binding
B0006725biological_processobsolete cellular aromatic compound metabolic process
B0016491molecular_functionoxidoreductase activity
B0019380biological_process3-phenylpropionate catabolic process
B0019439biological_processobsolete aromatic compound catabolic process
B0051213molecular_functiondioxygenase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 702
ChainResidue
BGLN563
BGLN565
BHOH771
BHOH780
BHOH851
BHOH861

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 707
ChainResidue
BLYS672
BHOH829
BGLY559
BSER560
BLYS664

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 717
ChainResidue
ALEU128
AASN129
ALYS130
ALYS131
AHOH1116

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE A 752
ChainResidue
AHIS208
AHIS213
AASP362
AHOH1182

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE FES A 751
ChainResidue
ACYS81
AHIS83
AARG84
ACYS101
AHIS104
ATRP106

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE IND A 708
ChainResidue
AASN201
AASP205
AHIS208
AHIS295
AASN297

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 Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:10669618, ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:9634695, ECO:0007744|PDB:1EG9, ECO:0007744|PDB:1NDO, ECO:0007744|PDB:1O7G, ECO:0007744|PDB:1O7H, ECO:0007744|PDB:1O7M, ECO:0007744|PDB:1O7N, ECO:0007744|PDB:1O7P, ECO:0007744|PDB:1O7W, ECO:0007744|PDB:1UUV, ECO:0007744|PDB:1UUW
ChainResidueDetails
ACYS81
AHIS83
ACYS101
AHIS104
AHIS208
AHIS213

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10669618, ECO:0000269|PubMed:12586937, ECO:0000269|PubMed:15942729, ECO:0000269|PubMed:9634695, ECO:0007744|PDB:1EG9, ECO:0007744|PDB:1NDO, ECO:0007744|PDB:1O7G, ECO:0007744|PDB:1O7H, ECO:0007744|PDB:1O7M, ECO:0007744|PDB:1O7N, ECO:0007744|PDB:1O7P, ECO:0007744|PDB:1O7W, ECO:0007744|PDB:1UUV
ChainResidueDetails
AASP362

site_idSWS_FT_FI3
Number of Residues1
DetailsSITE: Important for enantioselectivity => ECO:0000269|PubMed:10692370
ChainResidueDetails
APHE352

Catalytic Information from CSA
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

218853

PDB entries from 2024-04-24

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