1NJT
COMPLEX STRUCTURE OF HCMV PROTEASE AND A PEPTIDOMIMETIC INHIBITOR
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004252 | molecular_function | serine-type endopeptidase activity |
A | 0006508 | biological_process | proteolysis |
B | 0004252 | molecular_function | serine-type endopeptidase activity |
B | 0006508 | biological_process | proteolysis |
C | 0004252 | molecular_function | serine-type endopeptidase activity |
C | 0006508 | biological_process | proteolysis |
D | 0004252 | molecular_function | serine-type endopeptidase activity |
D | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL A 257 |
Chain | Residue |
A | ASN62 |
A | CYS161 |
A | SER162 |
A | ASN224 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL B 2 |
Chain | Residue |
B | ASN362 |
B | CYS461 |
B | SER462 |
B | ASN524 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL C 1 |
Chain | Residue |
C | CYS1161 |
C | SER1162 |
C | ASN1224 |
C | ASN1062 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE CL D 4 |
Chain | Residue |
D | ASN1362 |
D | CYS1461 |
D | SER1462 |
D | ASN1524 |
site_id | AC5 |
Number of Residues | 14 |
Details | BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR |
Chain | Residue |
A | GLU31 |
A | HIS63 |
A | SER132 |
A | LEU133 |
A | SER134 |
A | SER135 |
A | ARG136 |
A | ARG137 |
A | GLY164 |
A | ARG165 |
A | ARG166 |
A | HOH273 |
A | HOH276 |
E | HOH245 |
site_id | AC6 |
Number of Residues | 13 |
Details | BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR |
Chain | Residue |
B | HOH38 |
B | HOH74 |
B | GLU331 |
B | HIS363 |
B | SER432 |
B | LEU433 |
B | SER434 |
B | SER435 |
B | ARG436 |
B | ARG437 |
B | GLY464 |
B | ARG465 |
F | HOH98 |
site_id | AC7 |
Number of Residues | 12 |
Details | BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR |
Chain | Residue |
C | HOH244 |
C | GLU1031 |
C | HIS1063 |
C | SER1132 |
C | LEU1133 |
C | SER1134 |
C | SER1135 |
C | ARG1136 |
C | ARG1137 |
C | GLY1164 |
C | ARG1165 |
G | HOH97 |
site_id | AC8 |
Number of Residues | 12 |
Details | BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR |
Chain | Residue |
D | HOH70 |
D | GLU1331 |
D | HIS1363 |
D | SER1432 |
D | LEU1433 |
D | SER1434 |
D | SER1435 |
D | ARG1436 |
D | ARG1437 |
D | GLY1464 |
D | ARG1465 |
H | HOH140 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
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 | |
C | HIS1063 | |
C | SER1132 | |
D | HIS1363 | |
D | SER1432 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | ACT_SITE: Charge relay system => ECO:0000255|HAMAP-Rule:MF_04008 |
Chain | Residue | Details |
A | HIS157 | |
B | HIS457 | |
C | HIS1157 | |
D | HIS1457 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | SITE: Cleavage; by assemblin; Internal site => ECO:0000269|PubMed:12163586 |
Chain | Residue | Details |
A | GLN143 | |
B | GLN443 | |
C | GLN1143 | |
D | GLN1443 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | SITE: Cleavage; by assemblin; Cryptic site => ECO:0000269|PubMed:12163586 |
Chain | Residue | Details |
A | ALA209 | |
B | ALA509 | |
C | ALA1209 | |
D | ALA1509 |
site_id | SWS_FT_FI5 |
Number of Residues | 4 |
Details | SITE: Cleavage; by assemblin; Release site => ECO:0000255|HAMAP-Rule:MF_04008 |
Chain | Residue | Details |
A | ALA256 | |
B | ALA556 | |
C | ALA1256 | |
D | ALA1556 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1nkk |
Chain | Residue | Details |
A | HIS157 | |
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 | HIS457 |
site_id | CSA3 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1nkk |
Chain | Residue | Details |
C | HIS1157 | |
C | SER1132 | |
C | ARG1165 | |
C | HIS1063 |
site_id | CSA4 |
Number of Residues | 4 |
Details | Annotated By Reference To The Literature 1nkk |
Chain | Residue | Details |
D | HIS1457 | |
D | ARG1465 | |
D | HIS1363 | |
D | SER1432 |
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 | HIS157 | 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 | HIS457 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
B | ARG465 | electrostatic stabiliser, hydrogen bond donor |
B | ARG466 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 238 |
Chain | Residue | Details |
C | HIS1063 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
C | SER1132 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
C | SER1134 | hydrogen bond donor, increase acidity, increase basicity |
C | HIS1157 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
C | ARG1165 | electrostatic stabiliser, hydrogen bond donor |
C | ARG1166 | electrostatic stabiliser, hydrogen bond donor |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 238 |
Chain | Residue | Details |
D | HIS1363 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
D | SER1432 | covalently attached, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
D | SER1434 | hydrogen bond donor, increase acidity, increase basicity |
D | HIS1457 | electrostatic stabiliser, hydrogen bond acceptor, increase acidity, increase basicity |
D | ARG1465 | electrostatic stabiliser, hydrogen bond donor |
D | ARG1466 | electrostatic stabiliser, hydrogen bond donor |