2SFP
ALANINE RACEMASE WITH BOUND PROPIONATE INHIBITOR
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 | 14 |
| Details | BINDING SITE FOR RESIDUE PLP A 500 |
| Chain | Residue |
| A | HIS166 |
| A | ASN203 |
| A | SER204 |
| A | ARG219 |
| A | GLY221 |
| A | ILE222 |
| A | TYR354 |
| A | HOH512 |
| A | HOH543 |
| A | HOH557 |
| B | PPI400 |
| A | LYS39 |
| A | TYR43 |
| A | ARG136 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PPI B 400 |
| Chain | Residue |
| A | LYS39 |
| A | ARG136 |
| A | TYR354 |
| A | PLP500 |
| B | TYR265 |
| B | CYS311 |
| B | MET312 |
| B | HOH505 |
| B | HOH582 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE PLP B 500 |
| Chain | Residue |
| A | PPI400 |
| B | LYS39 |
| B | TYR43 |
| B | ARG136 |
| B | HIS166 |
| B | SER204 |
| B | ARG219 |
| B | GLY221 |
| B | ILE222 |
| B | TYR354 |
| B | HOH537 |
| B | HOH551 |
| B | HOH581 |
| site_id | AC4 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PPI A 400 |
| Chain | Residue |
| A | TYR265 |
| A | TYR284 |
| A | CYS311 |
| A | MET312 |
| A | HOH569 |
| A | HOH570 |
| B | LYS39 |
| B | ARG136 |
| B | TYR354 |
| B | PLP500 |
| site_id | KC1 |
| Number of Residues | 1 |
| Details | CARBAMYLATED LYSINE |
| Chain | Residue |
| A | KCX129 |
| site_id | KC2 |
| Number of Residues | 1 |
| Details | CARBAMYLATED LYSINE |
| Chain | Residue |
| B | KCX129 |
| site_id | PL1 |
| Number of Residues | 1 |
| Details | PYRIDOXAL-5-PHOSPHATE COFACTOR |
| Chain | Residue |
| A | PLP500 |
| site_id | PL2 |
| Number of Residues | 1 |
| Details | PYRIDOXAL-5-PHOSPHATE COFACTOR |
| Chain | Residue |
| B | PLP500 |
| site_id | PP1 |
| Number of Residues | 1 |
| Details | PROPIONATE INHIBITOR |
| Chain | Residue |
| B | PPI400 |
| site_id | PP2 |
| Number of Residues | 1 |
| Details | PROPIONATE INHIBITOR |
| Chain | Residue |
| A | PPI400 |
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 | ACT_SITE: Proton acceptor; specific for D-alanine => ECO:0000305|PubMed:10502689, ECO:0000305|PubMed:15807525 |
| Chain | Residue | Details |
| A | LYS39 | |
| B | LYS39 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor; specific for L-alanine => ECO:0000305|PubMed:10502689, ECO:0000305|PubMed:15807525 |
| Chain | Residue | Details |
| A | TYR265 | |
| B | TYR265 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11886871 |
| Chain | Residue | Details |
| A | ARG136 | |
| A | MET312 | |
| B | ARG136 | |
| B | MET312 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:11886871, ECO:0000269|PubMed:15807525, ECO:0000269|PubMed:9063881 |
| Chain | Residue | Details |
| A | LYS39 | |
| B | LYS39 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:10079072, ECO:0000269|PubMed:11886871, ECO:0000269|PubMed:12741835, ECO:0000269|PubMed:15807525, ECO:0000269|Ref.10 |
| Chain | Residue | Details |
| A | KCX129 | |
| B | KCX129 |
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 | ARG136 | electrostatic stabiliser |
| A | HIS166 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| A | ARG219 | electrostatic stabiliser, hydrogen bond donor |
| A | TYR265 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | CYS311 | electrostatic stabiliser |
| A | ASP313 | 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 | ARG136 | electrostatic stabiliser |
| B | HIS166 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
| B | ARG219 | electrostatic stabiliser, hydrogen bond donor |
| B | TYR265 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | CYS311 | electrostatic stabiliser |
| B | ASP313 | electrostatic stabiliser, hydrogen bond acceptor |
