4QUQ
Crystal structure of stachydrine demethylase in complex with azide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051537 | molecular_function | 2 iron, 2 sulfur cluster binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE FES A 501 |
| Chain | Residue |
| A | CYS86 |
| A | HIS88 |
| A | ARG89 |
| A | SER91 |
| A | CYS106 |
| A | HIS109 |
| A | GLN110 |
| A | TRP111 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE FE A 502 |
| Chain | Residue |
| A | HIS209 |
| A | ASP360 |
| A | AZI505 |
| A | HIS204 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 503 |
| Chain | Residue |
| A | ARG15 |
| A | LEU16 |
| A | GLU22 |
| A | HOH612 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE NCO A 504 |
| Chain | Residue |
| A | LEU12 |
| A | LEU12 |
| A | ASP13 |
| A | ASP13 |
| A | ARG15 |
| A | ARG15 |
| A | GLU401 |
| A | HOH684 |
| A | HOH708 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE AZI A 505 |
| Chain | Residue |
| A | ASN199 |
| A | GLU201 |
| A | CYS202 |
| A | HIS209 |
| A | ASP360 |
| A | FE502 |
Functional Information from PROSITE/UniProt
| site_id | PS00570 |
| Number of Residues | 24 |
| Details | RING_HYDROXYL_ALPHA Bacterial ring hydroxylating dioxygenases alpha-subunit signature. CrHRGslickarqGQvaklvCpYH |
| Chain | Residue | Details |
| A | CYS86-HIS109 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 105 |
| Details | Domain: {"description":"Rieske","evidences":[{"source":"PROSITE-ProRule","id":"PRU00628","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22224443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26996959","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2014","submissionDatabase":"PDB data bank","title":"Tracking photoelectron induced in-crystallo enzyme catalysis.","authors":["Agarwal R.","Andi B.","Gizzi A.","Bonanno J.B.","Almo S.C.","Orville A.M."]}},{"source":"PDB","id":"3VCA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VCP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5HL4","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22224443","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"26996959","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"JUL-2014","submissionDatabase":"PDB data bank","title":"Tracking photoelectron induced in-crystallo enzyme catalysis.","authors":["Agarwal R.","Andi B.","Gizzi A.","Bonanno J.B.","Almo S.C.","Orville A.M."]}},{"source":"PDB","id":"3VCA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3VCP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUQ","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4QUR","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
