1SJB
X-ray structure of o-succinylbenzoate synthase complexed with o-succinylbenzoic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0003824 | molecular_function | catalytic activity |
A | 0009234 | biological_process | menaquinone biosynthetic process |
A | 0016829 | molecular_function | lyase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0003824 | molecular_function | catalytic activity |
B | 0009234 | biological_process | menaquinone biosynthetic process |
B | 0016829 | molecular_function | lyase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
B | 0046872 | molecular_function | metal ion binding |
C | 0003824 | molecular_function | catalytic activity |
C | 0009234 | biological_process | menaquinone biosynthetic process |
C | 0016829 | molecular_function | lyase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0043748 | molecular_function | O-succinylbenzoate synthase activity |
C | 0046872 | molecular_function | metal ion binding |
D | 0003824 | molecular_function | catalytic activity |
D | 0009234 | biological_process | menaquinone biosynthetic process |
D | 0016829 | molecular_function | lyase activity |
D | 0016853 | molecular_function | isomerase 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 | ACT_SITE: Proton donor => ECO:0000305|PubMed:14705949, ECO:0000305|PubMed:15134446 |
Chain | Residue | Details |
A | LYS163 | |
B | LYS163 | |
C | LYS163 | |
D | LYS163 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:14705949, ECO:0000305|PubMed:15134446 |
Chain | Residue | Details |
A | LYS263 | |
B | LYS263 | |
C | LYS263 | |
D | LYS263 |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15134446, ECO:0007744|PDB:1SJB |
Chain | Residue | Details |
D | SER135 | |
D | LYS161 | |
D | ASN191 | |
D | ILE293 | |
A | SER135 | |
A | LYS161 | |
A | ASN191 | |
A | ILE293 | |
B | SER135 | |
B | LYS161 | |
B | ASN191 | |
B | ILE293 | |
C | SER135 | |
C | LYS161 | |
C | ASN191 | |
C | ILE293 |
site_id | SWS_FT_FI4 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15134446, ECO:0000269|PubMed:23130969, ECO:0000269|Ref.9, ECO:0007744|PDB:1SJA, ECO:0007744|PDB:1SJB, ECO:0007744|PDB:1SJC, ECO:0007744|PDB:4A6G, ECO:0007744|PDB:5FJO, ECO:0007744|PDB:5FJP, ECO:0007744|PDB:5FJR, ECO:0007744|PDB:5FJT, ECO:0007744|PDB:5FJU |
Chain | Residue | Details |
C | ASP239 | |
D | ASP189 | |
D | GLU214 | |
D | ASP239 | |
A | ASP189 | |
A | GLU214 | |
A | ASP239 | |
B | ASP189 | |
B | GLU214 | |
B | ASP239 | |
C | ASP189 | |
C | GLU214 |