1JJU
Structure of a Quinohemoprotein Amine Dehydrogenase with a Unique Redox Cofactor and Highly Unusual Crosslinking
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0009055 | molecular_function | electron transfer activity |
A | 0020037 | molecular_function | heme binding |
A | 0046872 | molecular_function | metal ion binding |
C | 0016491 | molecular_function | oxidoreductase activity |
C | 0016638 | molecular_function | oxidoreductase activity, acting on the CH-NH2 group of donors |
C | 0042597 | cellular_component | periplasmic space |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE NA C 996 |
Chain | Residue |
B | PHE244 |
B | HOH1167 |
C | ASP12 |
C | ASP33 |
C | TRQ43 |
C | TBU993 |
site_id | AC2 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE HEM A 991 |
Chain | Residue |
A | HIS15 |
A | ARG25 |
A | ILE26 |
A | THR39 |
A | ARG42 |
A | MET43 |
A | HIS47 |
A | VAL49 |
A | ARG114 |
A | PHE125 |
A | HEM992 |
A | HOH1139 |
A | HOH1267 |
B | LEU107 |
B | THR108 |
B | HIS109 |
A | ALA10 |
A | CYS11 |
A | CYS14 |
site_id | AC3 |
Number of Residues | 24 |
Details | BINDING SITE FOR RESIDUE HEM A 992 |
Chain | Residue |
A | LYS31 |
A | THR39 |
A | ARG42 |
A | ARG45 |
A | THR99 |
A | CYS100 |
A | ARG102 |
A | CYS103 |
A | HIS104 |
A | ARG108 |
A | VAL109 |
A | GLN112 |
A | ARG114 |
A | LEU122 |
A | HIS126 |
A | PHE130 |
A | GLN136 |
A | LEU156 |
A | HEM991 |
A | HOH996 |
A | HOH1001 |
A | HOH1007 |
A | HOH1008 |
A | HOH1059 |
site_id | AC4 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE TBU C 993 |
Chain | Residue |
B | PHE244 |
C | ASP12 |
C | GLY36 |
C | TRP42 |
C | TRQ43 |
C | NA996 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE TBU B 994 |
Chain | Residue |
B | GLU132 |
site_id | AC6 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE TBU A 995 |
Chain | Residue |
A | ASP257 |
A | ILE263 |
A | HOH1119 |
B | ARG128 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"12925784","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11717396","evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI8 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Tryptophylquinone","evidences":[{"source":"PubMed","id":"11717396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12925784","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI9 |
Number of Residues | 2 |
Details | Cross-link: {"description":"4-cysteinyl-glutamic acid (Cys-Glu)","evidences":[{"source":"PubMed","id":"11717396","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI10 |
Number of Residues | 2 |
Details | Cross-link: {"description":"3-cysteinyl-aspartic acid (Cys-Asp)","evidences":[{"source":"PubMed","id":"11717396","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI11 |
Number of Residues | 2 |
Details | Cross-link: {"description":"4'-cysteinyl-tryptophylquinone (Cys-Trp)","evidences":[{"source":"PubMed","id":"11717396","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12925784","evidenceCode":"ECO:0000269"}]} |
Chain | Residue | Details |