1XQL
Effect of a Y265F Mutant on the Transamination Based Cycloserine Inactivation of Alanine Racemase
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 PMP A 501 |
Chain | Residue |
A | LYS39 |
A | TYR354 |
A | HOH661 |
A | HOH670 |
A | HOH695 |
B | PHE265 |
A | TYR43 |
A | ARG136 |
A | HIS166 |
A | ASN203 |
A | SER204 |
A | ARG219 |
A | GLY221 |
A | ILE222 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE PMH A 503 |
Chain | Residue |
A | LYS39 |
A | TYR43 |
A | KCX129 |
A | ARG136 |
A | HIS166 |
A | ASN203 |
A | SER204 |
A | ARG219 |
A | GLY221 |
A | ILE222 |
A | TYR354 |
A | HOH661 |
A | HOH670 |
A | HOH695 |
A | HOH697 |
B | PHE265 |
B | TYR284 |
B | CYS311 |
B | MET312 |
B | HOH672 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLP A 504 |
Chain | Residue |
A | LYS39 |
A | TYR43 |
A | LEU85 |
A | HIS166 |
A | ASN203 |
A | SER204 |
A | ARG219 |
A | GLY221 |
A | ILE222 |
A | TYR354 |
A | HOH661 |
A | HOH670 |
A | HOH695 |
site_id | AC4 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 4AX B 505 |
Chain | Residue |
A | LYS39 |
A | ARG136 |
A | PLP504 |
A | HOH697 |
B | PHE265 |
B | TYR284 |
B | CYS311 |
B | MET312 |
B | HOH672 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR RESIDUE PMP B 601 |
Chain | Residue |
B | VAL37 |
B | LYS39 |
B | TYR43 |
B | ARG136 |
B | HIS166 |
B | ASN203 |
B | SER204 |
B | ARG219 |
B | GLY221 |
B | ILE222 |
B | TYR354 |
B | HOH605 |
B | HOH643 |
B | HOH678 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE PMH B 603 |
Chain | Residue |
A | PHE265 |
A | TYR284 |
A | CYS311 |
A | MET312 |
A | HOH678 |
B | LYS39 |
B | TYR43 |
B | ARG136 |
B | HIS166 |
B | ASN203 |
B | SER204 |
B | ARG219 |
B | GLY221 |
B | ILE222 |
B | TYR354 |
B | HOH605 |
B | HOH628 |
B | HOH643 |
B | HOH678 |
site_id | AC7 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PLP B 604 |
Chain | Residue |
B | TYR354 |
B | HOH605 |
B | HOH678 |
B | LYS39 |
B | TYR43 |
B | LEU85 |
B | ARG136 |
B | HIS166 |
B | ASN203 |
B | SER204 |
B | ARG219 |
B | GLY221 |
B | ILE222 |
site_id | AC8 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE 4AX A 605 |
Chain | Residue |
A | PHE265 |
A | TYR284 |
A | MET312 |
A | HOH678 |
A | HOH746 |
B | LYS39 |
B | ARG136 |
B | TYR354 |
B | HOH628 |
site_id | AC9 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY B 502 |
Chain | Residue |
A | LYS39 |
A | ARG136 |
B | PHE265 |
B | CYS311 |
B | MET312 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE ACY A 602 |
Chain | Residue |
A | PHE265 |
A | CYS311 |
A | MET312 |
B | LYS39 |
B | ARG136 |
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 | PHE265 | |
B | PHE265 |
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 | PHE265 | |
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 | PHE265 |
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 | PHE265 | 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 | PHE265 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | CYS311 | electrostatic stabiliser |
B | ASP313 | electrostatic stabiliser, hydrogen bond acceptor |