5FJP
N-acyl amino acid racemase from Amycolatopsis sp Ts-1-60: G291D F323Y I293G mutant in complex with N-acetyl naphthylalanine
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 | 15 |
Details | BINDING SITE FOR RESIDUE NPQ B 1369 |
Chain | Residue |
B | PHE19 |
B | LYS263 |
B | ASP291 |
B | ASP316 |
B | TYR323 |
B | MG1370 |
B | HOH2051 |
B | GLN26 |
B | MET50 |
B | SER135 |
B | LYS161 |
B | LYS163 |
B | ASP189 |
B | ASN191 |
B | ASP239 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NPQ D 1368 |
Chain | Residue |
D | PHE19 |
D | GLN26 |
D | MET50 |
D | SER135 |
D | LYS161 |
D | LYS163 |
D | ASP189 |
D | ASN191 |
D | GLU214 |
D | ASP239 |
D | LYS263 |
D | ASP291 |
D | ASP316 |
D | TYR323 |
D | MG1369 |
D | HOH2028 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NPQ C 1368 |
Chain | Residue |
C | PHE19 |
C | GLN26 |
C | SER135 |
C | LYS161 |
C | LYS163 |
C | ASP189 |
C | ASN191 |
C | ASP239 |
C | LYS263 |
C | ASP291 |
C | MET292 |
C | TYR323 |
C | MG1369 |
site_id | AC4 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE NPQ A 1369 |
Chain | Residue |
A | PHE19 |
A | GLN26 |
A | SER135 |
A | LYS161 |
A | LYS163 |
A | ASP189 |
A | ASN191 |
A | LYS263 |
A | ASP291 |
A | ASP316 |
A | TYR323 |
A | MG1370 |
A | HOH2055 |
site_id | AC5 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG A 1370 |
Chain | Residue |
A | LYS161 |
A | ASP189 |
A | ASN191 |
A | GLU214 |
A | ASP239 |
A | NPQ1369 |
A | HOH2062 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG B 1370 |
Chain | Residue |
B | ASP189 |
B | GLU214 |
B | ASP239 |
B | NPQ1369 |
B | HOH2056 |
site_id | AC7 |
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 | HOH2037 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG D 1369 |
Chain | Residue |
D | LYS161 |
D | ASP189 |
D | GLU214 |
D | ASP239 |
D | NPQ1368 |
D | HOH2031 |
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 |
A | SER135 | |
C | LYS161 | |
C | ASN191 | |
C | GLY293 | |
D | SER135 | |
D | LYS161 | |
D | ASN191 | |
D | GLY293 | |
A | LYS161 | |
A | ASN191 | |
A | GLY293 | |
B | SER135 | |
B | LYS161 | |
B | ASN191 | |
B | GLY293 | |
C | SER135 |
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 |
A | ASP189 | |
D | ASP189 | |
D | GLU214 | |
D | ASP239 | |
A | GLU214 | |
A | ASP239 | |
B | ASP189 | |
B | GLU214 | |
B | ASP239 | |
C | ASP189 | |
C | GLU214 | |
C | ASP239 |