1FTX
Crystal structure of alanine racemase in complex with D-alanine phosphonate
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE EPC A 1001 |
| Chain | Residue |
| A | VAL37 |
| A | ILE222 |
| A | TYR354 |
| A | HOH445 |
| A | HOH457 |
| A | HOH504 |
| A | HOH543 |
| A | HOH555 |
| B | TYR265 |
| B | TYR284 |
| B | CYS311 |
| A | LYS39 |
| B | MET312 |
| B | ASP313 |
| A | TYR43 |
| A | ARG136 |
| A | HIS166 |
| A | ASN203 |
| A | SER204 |
| A | ARG219 |
| A | GLY221 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE EPC B 1002 |
| Chain | Residue |
| A | TYR265 |
| A | CYS311 |
| A | MET312 |
| A | ASP313 |
| B | LYS39 |
| B | TYR43 |
| B | KCX129 |
| B | ARG136 |
| B | HIS166 |
| B | ASN203 |
| B | SER204 |
| B | ARG219 |
| B | GLY221 |
| B | ILE222 |
| B | TYR354 |
| B | HOH405 |
| B | HOH467 |
| B | HOH505 |
| B | HOH550 |
| B | HOH573 |
Functional Information from PROSITE/UniProt
| site_id | PS00395 |
| Number of Residues | 11 |
| Details | ALANINE_RACEMASE Alanine racemase pyridoxal-phosphate attachment site. AVvKANAYGHG |
| Chain | Residue | Details |
| A | ALA36-GLY46 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| 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 | 2 |
| 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 | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11886871","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| 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 | 2 |
| 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 | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | CYS311 | |
| A | TYR265 | |
| B | ARG136 | |
| B | LYS39 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1bd0 |
| Chain | Residue | Details |
| A | ARG136 | |
| A | LYS39 | |
| B | CYS311 | |
| B | TYR265 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 213 |
| Chain | Residue | Details |
| A | LYS39 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | LYS140 | electrostatic stabiliser |
| A | ALA170 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | ALA223 | electrostatic stabiliser, hydrogen bond donor |
| A | TYR269 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | CYS315 | electrostatic stabiliser |
| A | ILE317 | electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 213 |
| Chain | Residue | Details |
| B | LYS39 | covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | LYS140 | electrostatic stabiliser |
| B | ALA170 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | ALA223 | electrostatic stabiliser, hydrogen bond donor |
| B | TYR269 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | CYS315 | electrostatic stabiliser |
| B | ILE317 | electrostatic stabiliser, hydrogen bond acceptor |
