5FJR
N-acyl amino acid racemase from Amycolatopsis sp. Ts-1-60: Q26A M50I G291D F323Y mutant in complex with N-acetyl napthylalanine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0009234 | biological_process | menaquinone biosynthetic process |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0016854 | molecular_function | racemase and epimerase activity |
| A | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0009234 | biological_process | menaquinone biosynthetic process |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0016854 | molecular_function | racemase and epimerase activity |
| B | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0009234 | biological_process | menaquinone biosynthetic process |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0016854 | molecular_function | racemase and epimerase activity |
| C | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0009234 | biological_process | menaquinone biosynthetic process |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016853 | molecular_function | isomerase activity |
| D | 0016854 | molecular_function | racemase and epimerase activity |
| D | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NPQ B 1368 |
| Chain | Residue |
| B | PHE19 |
| B | ASP239 |
| B | LYS263 |
| B | ASP291 |
| B | MET292 |
| B | ILE293 |
| B | MG1369 |
| B | PHE23 |
| B | ALA26 |
| B | ARG29 |
| B | ILE50 |
| B | SER135 |
| B | LYS161 |
| B | LYS163 |
| B | ASN191 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE NPQ D 1368 |
| Chain | Residue |
| D | PHE19 |
| D | ILE50 |
| D | SER135 |
| D | LYS161 |
| D | LYS163 |
| D | ASN191 |
| D | ASP239 |
| D | LYS263 |
| D | ASP291 |
| D | MET292 |
| D | ASP316 |
| D | MG1369 |
| D | HOH2051 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE NPQ C 1368 |
| Chain | Residue |
| C | PHE19 |
| C | PHE23 |
| C | ILE50 |
| C | SER135 |
| C | LYS161 |
| C | LYS163 |
| C | ASP189 |
| C | ASN191 |
| C | GLU214 |
| C | ASP239 |
| C | LYS263 |
| C | ASP291 |
| C | MET292 |
| C | MG1369 |
| site_id | AC4 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE NPQ A 1369 |
| Chain | Residue |
| A | PHE19 |
| A | PHE23 |
| A | ALA26 |
| A | ILE50 |
| A | SER135 |
| A | LYS161 |
| A | LYS163 |
| A | ASP189 |
| A | ASN191 |
| A | GLU214 |
| A | ASP239 |
| A | LYS263 |
| A | ASP291 |
| A | MET292 |
| A | ILE293 |
| A | TYR323 |
| A | MG1370 |
| A | HOH2137 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG D 1369 |
| Chain | Residue |
| D | ASP189 |
| D | GLU214 |
| D | ASP239 |
| D | NPQ1368 |
| D | HOH2059 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1370 |
| Chain | Residue |
| A | ASP189 |
| A | ASN191 |
| A | GLU214 |
| A | ASP239 |
| A | NPQ1369 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1369 |
| Chain | Residue |
| B | ASP189 |
| B | ASN191 |
| B | GLU214 |
| B | ASP239 |
| B | NPQ1368 |
| B | HOH2080 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 1369 |
| Chain | Residue |
| C | ASP189 |
| C | ASN191 |
| C | GLU214 |
| C | ASP239 |
| C | NPQ1368 |
| C | HOH2066 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton donor","evidences":[{"source":"PubMed","id":"14705949","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15134446","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"14705949","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15134446","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15134446","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1SJB","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"15134446","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23130969","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"OCT-2015","submissionDatabase":"PDB data bank","title":"Structure of N-Acylamino Acid Racemase Mutants in Complex with Substrates.","authors":["Sanchez-Carron G.","Campopiano D.","Grogan G."]}},{"source":"PDB","id":"1SJA","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SJB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1SJC","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4A6G","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FJO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FJP","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FJR","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FJT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5FJU","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
