5FJO
N-acyl amino acid racemase from Amycolatopsis sp. Ts-1-60: G291D- F323Y 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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NPQ B 1369 |
Chain | Residue |
B | PHE19 |
B | ASP239 |
B | LYS263 |
B | ASP291 |
B | ILE293 |
B | TYR323 |
B | MG1370 |
B | HOH2265 |
B | GLN26 |
B | ARG29 |
B | MET50 |
B | SER135 |
B | LYS161 |
B | LYS163 |
B | ASP189 |
B | ASN191 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE NPQ A 1368 |
Chain | Residue |
A | PHE19 |
A | GLN26 |
A | ARG29 |
A | MET50 |
A | SER135 |
A | LYS161 |
A | LYS163 |
A | ASP189 |
A | ASN191 |
A | ASP239 |
A | LYS263 |
A | ASP291 |
A | ILE293 |
A | TYR323 |
A | MG1369 |
A | HOH2266 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG B 1370 |
Chain | Residue |
B | LYS161 |
B | ASP189 |
B | GLU214 |
B | ASP239 |
B | NPQ1369 |
B | HOH2292 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1369 |
Chain | Residue |
A | ASP189 |
A | GLU214 |
A | ASP239 |
A | NPQ1368 |
A | HOH2295 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:14705949, ECO:0000305|PubMed:15134446 |
Chain | Residue | Details |
A | LYS163 | |
B | LYS163 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:14705949, ECO:0000305|PubMed:15134446 |
Chain | Residue | Details |
A | LYS263 | |
B | LYS263 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000269|PubMed:15134446, ECO:0007744|PDB:1SJB |
Chain | Residue | Details |
A | SER135 | |
A | LYS161 | |
A | ASN191 | |
A | ILE293 | |
B | SER135 | |
B | LYS161 | |
B | ASN191 | |
B | ILE293 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
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 | |
A | GLU214 | |
A | ASP239 | |
B | ASP189 | |
B | GLU214 | |
B | ASP239 |