1XPY
Structural Basis for Catalytic Racemization and Substrate Specificity of an N-Acylamino Acid Racemase Homologue from Deinococcus radiodurans
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 | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 1377 |
| Chain | Residue |
| A | LYS168 |
| A | ASP195 |
| A | GLU220 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG B 2377 |
| Chain | Residue |
| B | LYS168 |
| B | ASP195 |
| B | GLU220 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG C 3377 |
| Chain | Residue |
| C | GLU220 |
| C | ASP245 |
| C | NLQ3376 |
| C | LYS168 |
| C | LYS170 |
| C | ASP195 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG D 4377 |
| Chain | Residue |
| D | LYS170 |
| D | ASP195 |
| D | ASN197 |
| D | GLU220 |
| D | ASP245 |
| D | NLQ4376 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE NLQ C 3376 |
| Chain | Residue |
| C | PHE26 |
| C | THR28 |
| C | PHE30 |
| C | SER142 |
| C | LYS168 |
| C | LYS170 |
| C | ASP195 |
| C | LYS269 |
| C | GLY297 |
| C | MET298 |
| C | LEU299 |
| C | ASP322 |
| C | TYR329 |
| C | MG3377 |
| C | HOH3378 |
| C | HOH3546 |
| site_id | AC6 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE NLQ D 4376 |
| Chain | Residue |
| D | PHE26 |
| D | PHE30 |
| D | SER142 |
| D | LYS168 |
| D | LYS170 |
| D | LYS269 |
| D | GLY297 |
| D | MET298 |
| D | LEU299 |
| D | ASP322 |
| D | TYR329 |
| D | MG4377 |
| D | HOH4412 |
| D | HOH4445 |
| D | HOH4555 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:15313614 |
| Chain | Residue | Details |
| A | LYS170 | |
| B | LYS170 | |
| C | LYS170 | |
| D | LYS170 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:15313614 |
| Chain | Residue | Details |
| A | LYS269 | |
| B | LYS269 | |
| C | LYS269 | |
| D | LYS269 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15313614, ECO:0007744|PDB:1XPY |
| Chain | Residue | Details |
| A | SER142 | |
| C | LYS168 | |
| C | LYS269 | |
| C | LEU299 | |
| D | SER142 | |
| D | LYS168 | |
| D | LYS269 | |
| D | LEU299 | |
| A | LYS168 | |
| A | LYS269 | |
| A | LEU299 | |
| B | SER142 | |
| B | LYS168 | |
| B | LYS269 | |
| B | LEU299 | |
| C | SER142 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15313614, ECO:0007744|PDB:1XPY, ECO:0007744|PDB:1XS2, ECO:0007744|PDB:2GGH |
| Chain | Residue | Details |
| A | ASP195 | |
| A | GLU220 | |
| B | ASP195 | |
| B | GLU220 | |
| C | ASP195 | |
| C | GLU220 | |
| D | ASP195 | |
| D | GLU220 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:15313614 |
| Chain | Residue | Details |
| A | ASP245 | |
| B | ASP245 | |
| C | ASP245 | |
| D | ASP245 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| A | LYS269 | |
| A | LYS168 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| B | LYS269 | |
| B | LYS168 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| C | LYS269 | |
| C | LYS168 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| D | LYS269 | |
| D | LYS168 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| A | LYS170 | |
| A | LYS269 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| B | LYS170 | |
| B | LYS269 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| C | LYS170 | |
| C | LYS269 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1r6w |
| Chain | Residue | Details |
| D | LYS170 | |
| D | LYS269 |
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 377 |
| Chain | Residue | Details |
| A | SER142 | transition state stabiliser |
| A | LYS168 | transition state stabiliser |
| A | LYS170 | proton donor |
| A | ASP195 | metal ligand |
| A | GLU220 | metal ligand |
| A | ASP245 | metal ligand |
| A | LYS269 | proton acceptor |
| A | GLY297 | transition state stabiliser |
| site_id | MCSA2 |
| Number of Residues | 8 |
| Details | M-CSA 377 |
| Chain | Residue | Details |
| B | SER142 | transition state stabiliser |
| B | LYS168 | transition state stabiliser |
| B | LYS170 | proton donor |
| B | ASP195 | metal ligand |
| B | GLU220 | metal ligand |
| B | ASP245 | metal ligand |
| B | LYS269 | proton acceptor |
| B | GLY297 | transition state stabiliser |
| site_id | MCSA3 |
| Number of Residues | 8 |
| Details | M-CSA 377 |
| Chain | Residue | Details |
| C | SER142 | transition state stabiliser |
| C | LYS168 | transition state stabiliser |
| C | LYS170 | proton donor |
| C | ASP195 | metal ligand |
| C | GLU220 | metal ligand |
| C | ASP245 | metal ligand |
| C | LYS269 | proton acceptor |
| C | GLY297 | transition state stabiliser |
| site_id | MCSA4 |
| Number of Residues | 8 |
| Details | M-CSA 377 |
| Chain | Residue | Details |
| D | SER142 | transition state stabiliser |
| D | LYS168 | transition state stabiliser |
| D | LYS170 | proton donor |
| D | ASP195 | metal ligand |
| D | GLU220 | metal ligand |
| D | ASP245 | metal ligand |
| D | LYS269 | proton acceptor |
| D | GLY297 | transition state stabiliser |
