2KT2
Structure of NmerA, the N-terminal HMA domain of Tn501 Mercuric Reductase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0046872 | molecular_function | metal ion binding |
Functional Information from PROSITE/UniProt
site_id | PS01047 |
Number of Residues | 30 |
Details | HMA_1 Heavy-metal-associated domain. ItGMtCdSCaahVKeaLekvpgvqsal.VsY |
Chain | Residue | Details |
A | ILE6-TYR35 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00280 |
Chain | Residue | Details |
A | CYS11 | |
A | CYS14 |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 4 |
Details | M-CSA 277 |
Chain | Residue | Details |
A | MET9 | electrostatic stabiliser, increase nucleophilicity, steric role |
A | CYS11 | activator, covalently attached, electrostatic stabiliser, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
A | CYS14 | activator, covalently attached, electrofuge, electrophile, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity, metal ligand, nucleofuge, nucleophile, proton acceptor, proton donor |
A | TYR62 | electrostatic stabiliser, hydrogen bond acceptor |