1ID4
CRYSTAL STRUCTURE OF THE CATALYTIC SITE MUTANT (H157Q) OF THE HUMAN CYTOMEGALOVIRUS PROTEASE
Functional Information from GO Data
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008, ECO:0000269|PubMed:8805706 |
| Chain | Residue | Details |
| A | HIS63 | |
| A | SER132 | |
| B | HIS363 | |
| B | SER432 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 |
| Chain | Residue | Details |
| A | GLN157 | |
| B | GLN457 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by assemblin; Internal site => ECO:0000269|PubMed:12163586 |
| Chain | Residue | Details |
| A | GLN143 | |
| B | GLN443 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by assemblin; Cryptic site => ECO:0000269|PubMed:12163586 |
| Chain | Residue | Details |
| A | ALA209 | |
| B | ALA509 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | SITE: Cleavage; by assemblin; Release site => ECO:0000255|HAMAP-Rule:MF_04008 |
| Chain | Residue | Details |
| A | ALA256 | |
| B | ALA556 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1nkk |
| Chain | Residue | Details |
| A | GLN157 | |
| A | HIS63 | |
| A | ARG165 | |
| A | SER132 |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | Annotated By Reference To The Literature 1nkk |
| Chain | Residue | Details |
| B | ARG465 | |
| B | SER432 | |
| B | HIS363 | |
| B | GLN457 |
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 238 |
| Chain | Residue | Details |
| A | HIS63 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | SER132 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | SER134 | hydrogen bond donor, increase acidity, increase basicity |
| A | GLN157 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
| A | ARG165 | electrostatic stabiliser, hydrogen bond donor |
| A | ARG166 | electrostatic stabiliser, hydrogen bond donor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 238 |
| Chain | Residue | Details |
| B | HIS363 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| B | SER432 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | SER434 | hydrogen bond donor, increase acidity, increase basicity |
| B | GLN457 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
| B | ARG465 | electrostatic stabiliser, hydrogen bond donor |
| B | ARG466 | electrostatic stabiliser, hydrogen bond donor |
