3UW6
Crystal Structure of Engineered Protein, Northeast Structural Genomics Consortium Target OR120
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005829 | cellular_component | cytosol |
| A | 0006522 | biological_process | alanine metabolic process |
| A | 0008784 | molecular_function | alanine racemase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030632 | biological_process | D-alanine biosynthetic process |
| B | 0003824 | molecular_function | catalytic activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006522 | biological_process | alanine metabolic process |
| B | 0008784 | molecular_function | alanine racemase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016853 | molecular_function | isomerase activity |
| B | 0030170 | molecular_function | pyridoxal phosphate binding |
| B | 0030632 | biological_process | D-alanine biosynthetic process |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0005829 | cellular_component | cytosol |
| C | 0006522 | biological_process | alanine metabolic process |
| C | 0008784 | molecular_function | alanine racemase activity |
| C | 0009252 | biological_process | peptidoglycan biosynthetic process |
| C | 0016853 | molecular_function | isomerase activity |
| C | 0030170 | molecular_function | pyridoxal phosphate binding |
| C | 0030632 | biological_process | D-alanine biosynthetic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor; specific for D-alanine","evidences":[{"source":"PubMed","id":"10502689","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15807525","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor; specific for L-alanine","evidences":[{"source":"PubMed","id":"10502689","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15807525","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11886871","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"source":"PubMed","id":"11886871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15807525","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9063881","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"10079072","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11886871","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12741835","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15807525","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"SEP-2000","submissionDatabase":"PDB data bank","title":"Crystal structure of alanine racemase in complex with D-alanine phosphonate.","authors":["Stamper G.F.","Ringe D."]}}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 213 |
| Chain | Residue | Details |
| A | ASP47 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | ILE152 | electrostatic stabiliser |
| A | TYR182 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | GLU243 | electrostatic stabiliser, hydrogen bond donor |
| A | GLN293 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | VAL339 | electrostatic stabiliser |
| A | SER341 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 213 |
| Chain | Residue | Details |
| B | ASP47 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | ILE152 | electrostatic stabiliser |
| B | TYR182 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | GLU243 | electrostatic stabiliser, hydrogen bond donor |
| B | GLN293 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | VAL339 | electrostatic stabiliser |
| B | SER341 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 213 |
| Chain | Residue | Details |
| C | ASP47 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | ILE152 | electrostatic stabiliser |
| C | TYR182 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| C | GLU243 | electrostatic stabiliser, hydrogen bond donor |
| C | GLN293 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| C | VAL339 | electrostatic stabiliser |
| C | SER341 | electrostatic stabiliser, hydrogen bond acceptor |
