2HMO
Crystal Structure of Naphthalene 1,2-Dioxygenase Bound to 3-Nitrotoluene.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0018625 | molecular_function | naphthalene 1,2-dioxygenase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051213 | molecular_function | dioxygenase activity |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019380 | biological_process | 3-phenylpropionate catabolic process |
| B | 0051213 | molecular_function | dioxygenase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 450 |
| Chain | Residue |
| A | HIS208 |
| A | HIS213 |
| A | ASP362 |
| A | HOH1059 |
| A | HOH1102 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 805 |
| Chain | Residue |
| A | HOH1143 |
| A | LEU128 |
| A | ASN129 |
| A | LYS130 |
| A | LYS131 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 810 |
| Chain | Residue |
| B | GLN63 |
| B | GLN65 |
| B | HOH881 |
| B | HOH912 |
| B | HOH946 |
| B | HOH949 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 811 |
| Chain | Residue |
| B | GLY59 |
| B | SER60 |
| B | GLU167 |
| B | LYS172 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 814 |
| Chain | Residue |
| A | LYS245 |
| A | TRP439 |
| A | HIS440 |
| A | EDO822 |
| A | HOH951 |
| A | HOH1039 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE FES A 815 |
| Chain | Residue |
| A | CYS81 |
| A | HIS83 |
| A | ARG84 |
| A | CYS101 |
| A | TYR103 |
| A | HIS104 |
| A | TRP106 |
| site_id | AC7 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE 3NT A 801 |
| Chain | Residue |
| A | ASN201 |
| A | PHE202 |
| A | ASP205 |
| A | VAL209 |
| A | VAL260 |
| A | HIS295 |
| A | ASN297 |
| A | TRP358 |
| A | HOH1059 |
| A | HOH1102 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO A 803 |
| Chain | Residue |
| A | LEU31 |
| A | PHE35 |
| A | ALA36 |
| A | MET59 |
| A | GLY60 |
| A | ILE61 |
| A | ASP62 |
| A | PHE152 |
| A | TYR376 |
| A | GLN377 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 804 |
| Chain | Residue |
| A | HIS18 |
| A | VAL80 |
| A | CYS81 |
| A | ARG82 |
| A | SER381 |
| A | ASP382 |
| A | HOH828 |
| A | HOH856 |
| A | HOH884 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 806 |
| Chain | Residue |
| B | TYR88 |
| B | GLN102 |
| B | MET191 |
| B | VAL192 |
| B | PHE193 |
| B | HOH836 |
| B | HOH850 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 807 |
| Chain | Residue |
| A | HOH1273 |
| B | ASN91 |
| B | GLN94 |
| B | HOH925 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 808 |
| Chain | Residue |
| B | ALA158 |
| B | GLU160 |
| B | PHE177 |
| B | VAL178 |
| B | ASP179 |
| B | HOH840 |
| B | HOH1003 |
| site_id | BC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO A 809 |
| Chain | Residue |
| A | PRO49 |
| A | ALA50 |
| A | ASP53 |
| A | HOH959 |
| A | HOH1210 |
| A | HOH1266 |
| B | ARG78 |
| B | TYR79 |
| B | LYS80 |
| B | LEU81 |
| site_id | BC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 812 |
| Chain | Residue |
| A | PRO118 |
| A | PHE119 |
| A | HOH1062 |
| A | HOH1204 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 813 |
| Chain | Residue |
| A | HOH1290 |
| B | GLU83 |
| B | ALA84 |
| B | ASN86 |
| B | HOH905 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 816 |
| Chain | Residue |
| A | TRP254 |
| A | TYR399 |
| A | LYS405 |
| A | HOH1280 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 817 |
| Chain | Residue |
| A | ARG342 |
| A | ASP346 |
| A | HOH845 |
| A | HOH1290 |
| B | ASN82 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO B 817 |
| Chain | Residue |
| A | ARG342 |
| B | ASN82 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 818 |
| Chain | Residue |
| A | ASP396 |
| A | VAL398 |
| A | HIS440 |
| A | HOH864 |
| A | HOH951 |
| A | HOH1011 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 819 |
| Chain | Residue |
| A | LYS136 |
| A | GLN377 |
| A | HOH836 |
| A | HOH1182 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO B 820 |
| Chain | Residue |
| B | LYS9 |
| B | LEU10 |
| B | VAL11 |
| B | SER12 |
| B | LYS113 |
| B | HOH991 |
| site_id | CC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 821 |
| Chain | Residue |
| A | THR56 |
| A | GLU92 |
| A | PRO186 |
| A | LYS188 |
| A | HOH1064 |
| A | HOH1218 |
| B | GLU70 |
| B | ARG183 |
| site_id | CC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 822 |
| Chain | Residue |
| A | GLY164 |
| A | ASP165 |
| A | SO4814 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 823 |
| Chain | Residue |
| A | LYS375 |
| A | HOH949 |
| A | HOH1330 |
| B | ASN150 |
Functional Information from PROSITE/UniProt
| site_id | PS00570 |
| Number of Residues | 24 |
| Details | RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGktlvsveaGNakgfvCsYH |
| Chain | Residue | Details |
| A | CYS81-HIS104 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 98 |
| Details | Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"16980501","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2012","submissionDatabase":"PDB data bank","title":"Naphthalene 1,2-Dioxygenase bound to thioanisole.","authors":["Ferraro D.J.","Ramaswamy S."]}},{"source":"PDB","id":"2HMJ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HMK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HML","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HMM","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HMN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"2HMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HJL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HKV","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HM0","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HM1","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HM2","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HM3","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HM4","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HM5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HM6","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HM7","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4HM8","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| A | HIS208 | |
| A | ASP205 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1ndo |
| Chain | Residue | Details |
| A | HIS104 |
