5FJU
N-acyl amino acid racemase from Amycolatopsis sp. Ts-1-60: Q26A M50I G291D F323Y mutant in complex with N-acetyl phenylalanine
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 B 1368 |
Chain | Residue |
B | ASP189 |
B | ASN191 |
B | GLU214 |
B | ASP239 |
B | GLU240 |
B | 5CR1369 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG C 1368 |
Chain | Residue |
C | ASP239 |
C | GLU240 |
C | 5CR1370 |
C | ASP189 |
C | ASN191 |
C | GLU214 |
site_id | AC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE MG D 1368 |
Chain | Residue |
D | ASP189 |
D | ASN191 |
D | GLU214 |
D | ASP239 |
D | GLU240 |
D | 5CR1370 |
D | HOH2063 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MG A 1369 |
Chain | Residue |
A | ASP189 |
A | ASN191 |
A | GLU214 |
A | ASP239 |
A | 5CR1370 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE 5CR A 1370 |
Chain | Residue |
A | PHE19 |
A | ILE50 |
A | SER135 |
A | LYS161 |
A | LYS163 |
A | ASP189 |
A | ASN191 |
A | GLU214 |
A | ASP239 |
A | LYS263 |
A | ASP291 |
A | MET292 |
A | TYR323 |
A | MG1369 |
site_id | AC6 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE 5CR C 1369 |
Chain | Residue |
C | GLY24 |
C | VAL28 |
C | ILE50 |
C | ALA51 |
C | GLY52 |
site_id | AC7 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 5CR D 1369 |
Chain | Residue |
D | GLY24 |
D | THR25 |
D | VAL28 |
D | GLU30 |
D | ILE50 |
D | ALA51 |
D | GLY52 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE 5CR A 1371 |
Chain | Residue |
A | THR25 |
A | ALA26 |
A | VAL28 |
A | ILE50 |
A | ALA51 |
A | GLY52 |
site_id | AC9 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE 5CR D 1370 |
Chain | Residue |
D | PHE19 |
D | ILE50 |
D | SER135 |
D | LYS161 |
D | LYS163 |
D | ASP189 |
D | ASN191 |
D | ASP239 |
D | LYS263 |
D | ASP291 |
D | MET292 |
D | ILE293 |
D | ASP316 |
D | TYR323 |
D | MG1368 |
D | HOH2063 |
site_id | BC1 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE 5CR C 1370 |
Chain | Residue |
C | PHE19 |
C | ILE50 |
C | SER135 |
C | LYS161 |
C | LYS163 |
C | ASP189 |
C | ASN191 |
C | GLU214 |
C | ASP239 |
C | LYS263 |
C | ASP291 |
C | MET292 |
C | ILE293 |
C | ASP316 |
C | TYR323 |
C | MG1368 |
site_id | BC2 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 5CR B 1369 |
Chain | Residue |
B | MET292 |
B | ILE293 |
B | TYR323 |
B | MG1368 |
B | PHE19 |
B | ILE50 |
B | SER135 |
B | LYS161 |
B | LYS163 |
B | ASP189 |
B | ASN191 |
B | GLU214 |
B | ASP239 |
B | LYS263 |
B | ASP291 |
site_id | BC3 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 5CR B 1370 |
Chain | Residue |
B | PHE23 |
B | GLY24 |
B | VAL28 |
B | ILE50 |
B | ALA51 |
B | GLY52 |
B | HOH2011 |
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 | ILE293 | |
D | SER135 | |
D | LYS161 | |
D | ASN191 | |
D | ILE293 | |
A | LYS161 | |
A | ASN191 | |
A | ILE293 | |
B | SER135 | |
B | LYS161 | |
B | ASN191 | |
B | ILE293 | |
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 |