1SJB
X-ray structure of o-succinylbenzoate synthase complexed with o-succinylbenzoic acid
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 | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 1001 |
| Chain | Residue |
| A | ASP189 |
| A | ASN191 |
| A | GLU214 |
| A | ASP239 |
| A | OSB1000 |
| A | HOH1116 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 1101 |
| Chain | Residue |
| B | ASP239 |
| B | OSB1100 |
| B | HOH1276 |
| B | LYS161 |
| B | ASP189 |
| B | GLU214 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG C 1201 |
| Chain | Residue |
| C | ASP189 |
| C | ASN191 |
| C | GLU214 |
| C | ASP239 |
| C | LYS263 |
| C | OSB1200 |
| C | HOH1343 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG D 1301 |
| Chain | Residue |
| D | ASP189 |
| D | ASN191 |
| D | GLU214 |
| D | ASP239 |
| D | LYS263 |
| D | OSB1300 |
| D | HOH1411 |
| site_id | AC5 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE OSB A 1000 |
| Chain | Residue |
| A | PHE23 |
| A | TYR55 |
| A | SER135 |
| A | LYS161 |
| A | LYS163 |
| A | ASP189 |
| A | ASN191 |
| A | ASP239 |
| A | LYS263 |
| A | GLY291 |
| A | MET292 |
| A | ILE293 |
| A | PHE323 |
| A | MG1001 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE OSB B 1100 |
| Chain | Residue |
| B | PHE19 |
| B | PHE23 |
| B | SER135 |
| B | LYS161 |
| B | LYS163 |
| B | ASP189 |
| B | ASN191 |
| B | ASP239 |
| B | LYS263 |
| B | GLY291 |
| B | MET292 |
| B | ILE293 |
| B | ASP316 |
| B | PHE323 |
| B | MG1101 |
| B | HOH1146 |
| B | HOH1147 |
| site_id | AC7 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE OSB C 1200 |
| Chain | Residue |
| C | PHE19 |
| C | PHE23 |
| C | TYR55 |
| C | SER135 |
| C | LYS161 |
| C | LYS163 |
| C | ASP189 |
| C | ASN191 |
| C | ASP239 |
| C | LYS263 |
| C | GLY291 |
| C | MET292 |
| C | ILE293 |
| C | ASP316 |
| C | PHE323 |
| C | MG1201 |
| C | HOH1366 |
| site_id | AC8 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE OSB D 1300 |
| Chain | Residue |
| D | PHE19 |
| D | PHE23 |
| D | TYR55 |
| D | SER135 |
| D | LYS161 |
| D | LYS163 |
| D | ASP189 |
| D | ASN191 |
| D | ASP239 |
| D | LYS263 |
| D | GLY291 |
| D | MET292 |
| D | ILE293 |
| D | PHE323 |
| D | MG1301 |
| D | HOH1431 |
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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| A | ASP316 | |
| A | LYS161 | |
| A | LYS163 |
| site_id | CSA10 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| B | LYS263 | |
| B | LYS163 |
| site_id | CSA11 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| C | LYS263 | |
| C | LYS163 |
| site_id | CSA12 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| D | LYS263 | |
| D | LYS163 |
| site_id | CSA2 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| B | ASP316 | |
| B | LYS161 | |
| B | LYS163 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| C | ASP316 | |
| C | LYS161 | |
| C | LYS163 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| D | ASP316 | |
| D | LYS161 | |
| D | LYS163 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| A | LYS161 | |
| A | LYS263 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| B | LYS161 | |
| B | LYS263 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| C | LYS161 | |
| C | LYS263 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| D | LYS161 | |
| D | LYS263 |
| site_id | CSA9 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1muc |
| Chain | Residue | Details |
| A | LYS263 | |
| A | LYS163 |
