2HML
Crystal Structure of the Naphthalene 1,2-Dioxygenase F352V Mutant Bound to Phenanthrene.
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 | PEY701 |
| A | HOH753 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 704 |
| Chain | Residue |
| A | HOH966 |
| A | LEU128 |
| A | ASN129 |
| A | LYS130 |
| A | LYS131 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 709 |
| Chain | Residue |
| B | GLN63 |
| B | GLN65 |
| B | HOH765 |
| B | HOH804 |
| B | HOH848 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 710 |
| Chain | Residue |
| B | GLY59 |
| B | SER60 |
| B | GLU167 |
| B | LYS172 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 713 |
| Chain | Residue |
| A | LYS245 |
| A | TRP439 |
| A | HIS440 |
| A | HOH884 |
| A | HOH928 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 B 714 |
| Chain | Residue |
| A | THR87 |
| A | SER90 |
| A | THR368 |
| A | HOH794 |
| A | HOH835 |
| A | HOH963 |
| B | ARG148 |
| B | HOH844 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE FES A 714 |
| Chain | Residue |
| A | CYS81 |
| A | HIS83 |
| A | ARG84 |
| A | CYS101 |
| A | HIS104 |
| A | TRP106 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PEY A 701 |
| Chain | Residue |
| A | ASN201 |
| A | ASP205 |
| A | HIS208 |
| A | VAL209 |
| A | ASN297 |
| A | FE450 |
| A | HOH734 |
| A | HOH753 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE EDO A 702 |
| Chain | Residue |
| A | LEU31 |
| A | PHE35 |
| A | ALA36 |
| A | MET59 |
| A | GLY60 |
| A | ILE61 |
| A | ASP62 |
| A | PHE152 |
| A | TYR376 |
| A | GLN377 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE EDO A 703 |
| Chain | Residue |
| A | HIS18 |
| A | VAL80 |
| A | CYS81 |
| A | ARG82 |
| A | SER381 |
| A | ASP382 |
| A | HOH732 |
| A | HOH798 |
| A | HOH808 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 705 |
| Chain | Residue |
| B | TYR88 |
| B | GLN102 |
| B | MET191 |
| B | VAL192 |
| B | PHE193 |
| B | HOH732 |
| B | HOH733 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 706 |
| Chain | Residue |
| B | ASN91 |
| B | GLN94 |
| B | HOH762 |
| B | HOH828 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 707 |
| Chain | Residue |
| B | ARG138 |
| B | ALA158 |
| B | GLU160 |
| B | PHE177 |
| B | VAL178 |
| B | ASP179 |
| B | HOH727 |
| site_id | BC5 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO B 708 |
| Chain | Residue |
| A | PRO49 |
| A | ALA50 |
| A | ASP53 |
| A | HOH847 |
| B | ARG78 |
| B | TYR79 |
| B | LYS80 |
| B | LEU81 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 711 |
| Chain | Residue |
| A | PRO118 |
| A | PHE119 |
| A | HOH892 |
| A | HOH1068 |
| site_id | BC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO B 712 |
| Chain | Residue |
| B | HOH849 |
| B | GLU83 |
| B | ALA84 |
| B | ASN86 |
| B | HOH797 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 715 |
| Chain | Residue |
| A | GLU24 |
| A | LYS374 |
| A | HOH756 |
| A | HOH931 |
| A | HOH958 |
| site_id | BC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 716 |
| Chain | Residue |
| A | THR56 |
| A | GLU92 |
| A | PRO186 |
| A | LYS188 |
| B | GLU70 |
| B | ARG183 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 717 |
| Chain | Residue |
| A | ARG342 |
| A | ASP346 |
| A | HOH747 |
| A | HOH890 |
| B | ASN82 |
| B | HOH849 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 718 |
| Chain | Residue |
| A | VAL190 |
| B | GLN186 |
| B | THR187 |
| B | HIS188 |
| site_id | CC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO B 719 |
| Chain | Residue |
| B | LEU10 |
| B | VAL11 |
| B | SER12 |
| B | LYS113 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A 720 |
| Chain | Residue |
| A | LYS136 |
| A | TYR376 |
| A | GLN377 |
| A | HOH758 |
| A | HOH1109 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 721 |
| Chain | Residue |
| A | SER73 |
| A | ILE74 |
| A | VAL141 |
| A | HOH967 |
| site_id | CC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 722 |
| Chain | Residue |
| A | VAL9 |
| A | SER10 |
| A | GLU11 |
| A | GLU442 |
| A | HOH846 |
| A | HOH1041 |
| site_id | CC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 723 |
| Chain | Residue |
| A | HIS29 |
| A | LYS32 |
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 |
