1QQ5
STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0016787 | molecular_function | hydrolase activity |
A | 0018784 | molecular_function | (S)-2-haloacid dehalogenase activity |
A | 0019120 | molecular_function | hydrolase activity, acting on acid halide bonds, in C-halide compounds |
B | 0016787 | molecular_function | hydrolase activity |
B | 0018784 | molecular_function | (S)-2-haloacid dehalogenase activity |
B | 0019120 | molecular_function | hydrolase activity, acting on acid halide bonds, in C-halide compounds |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE FMT B 1001 |
Chain | Residue |
B | ASP8 |
B | ALA9 |
B | TYR10 |
B | SER114 |
B | ASN115 |
B | LYS147 |
B | HOH742 |
site_id | AC2 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FMT A 1002 |
Chain | Residue |
A | TYR10 |
A | SER114 |
A | ASN115 |
A | LYS147 |
A | ASP8 |
A | ALA9 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000269|PubMed:10521454, ECO:0000269|PubMed:9407083 |
Chain | Residue | Details |
A | ASP8 | |
B | ASP8 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10521454, ECO:0000269|PubMed:9407083, ECO:0007744|PDB:1AQ6, ECO:0007744|PDB:1QQ5, ECO:0007744|PDB:1QQ6, ECO:0007744|PDB:1QQ7 |
Chain | Residue | Details |
A | ALA9 | |
A | SER114 | |
B | ALA9 | |
B | SER114 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000269|PubMed:10521454, ECO:0007744|PDB:1QQ6, ECO:0007744|PDB:1QQ7 |
Chain | Residue | Details |
A | ARG39 | |
B | ARG39 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | SITE: Important for catalytic activity => ECO:0000305|PubMed:10521454, ECO:0000305|PubMed:9407083 |
Chain | Residue | Details |
A | THR12 | |
A | LYS147 | |
A | TYR153 | |
B | THR12 | |
B | LYS147 | |
B | TYR153 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 9 |
Details | a catalytic site defined by CSA, PubMed 9614112, 10521454 |
Chain | Residue | Details |
A | ARG39 | |
A | THR12 | |
A | ASP176 | |
A | PHE175 | |
A | ASP8 | |
A | ASN173 | |
A | LYS147 | |
A | ASN115 | |
A | SER171 |
site_id | CSA2 |
Number of Residues | 9 |
Details | a catalytic site defined by CSA, PubMed 9614112, 10521454 |
Chain | Residue | Details |
B | ARG39 | |
B | THR12 | |
B | ASP176 | |
B | PHE175 | |
B | ASP8 | |
B | ASN173 | |
B | LYS147 | |
B | ASN115 | |
B | SER171 |
site_id | MCSA1 |
Number of Residues | 10 |
Details | M-CSA 36 |
Chain | Residue | Details |
A | ASP8 | hydrogen bond acceptor, nucleofuge, nucleophile |
A | ASP176 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
A | THR12 | electrostatic stabiliser, hydrogen bond donor |
A | ARG39 | electrostatic stabiliser, hydrogen bond donor |
A | SER114 | electrostatic stabiliser |
A | ASN115 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
A | LYS147 | activator, hydrogen bond donor |
A | SER171 | electrostatic stabiliser, hydrogen bond donor |
A | ASN173 | electrostatic stabiliser, hydrogen bond donor |
A | PHE175 | electrostatic stabiliser, polar/non-polar interaction |
site_id | MCSA2 |
Number of Residues | 10 |
Details | M-CSA 36 |
Chain | Residue | Details |
B | ASP8 | hydrogen bond acceptor, nucleofuge, nucleophile |
B | ASP176 | activator, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
B | THR12 | electrostatic stabiliser, hydrogen bond donor |
B | ARG39 | electrostatic stabiliser, hydrogen bond donor |
B | SER114 | electrostatic stabiliser |
B | ASN115 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor |
B | LYS147 | activator, hydrogen bond donor |
B | SER171 | electrostatic stabiliser, hydrogen bond donor |
B | ASN173 | electrostatic stabiliser, hydrogen bond donor |
B | PHE175 | electrostatic stabiliser, polar/non-polar interaction |