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Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1NKK

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	14
Details	BINDING SITE FOR CHAIN E OF PEPTIDOMIMETIC INHIBITOR

Chain	Residue
A	ARG31
A	GLY164
A	ARG165
A	HOH2051
A	HOH2246
E	HOH2138
A	HIS63
A	SER132
A	LEU133
A	SER134
A	SER135
A	ARG136
A	ARG137
A	CYS161

site_id	AC2
Number of Residues	15
Details	BINDING SITE FOR CHAIN F OF PEPTIDOMIMETIC INHIBITOR

Chain	Residue
B	ARG331
B	HIS363
B	SER432
B	LEU433
B	SER434
B	SER435
B	ARG436
B	ARG437
B	VAL463
B	GLY464
B	ARG465
B	ARG466
B	HOH2092
F	HOH2022
F	HOH2109

site_id	AC3
Number of Residues	14
Details	BINDING SITE FOR CHAIN G OF PEPTIDOMIMETIC INHIBITOR

Chain	Residue
C	ARG1031
C	HIS1063
C	SER1132
C	LEU1133
C	SER1134
C	SER1135
C	ARG1136
C	ARG1137
C	CYS1161
C	GLY1164
C	ARG1165
C	HOH2098
C	HOH2127
G	HOH2073

site_id	AC4
Number of Residues	16
Details	BINDING SITE FOR CHAIN H OF PEPTIDOMIMETIC INHIBITOR

Chain	Residue
D	ARG1331
D	HIS1363
D	LEU1431
D	SER1432
D	LEU1433
D	SER1434
D	SER1435
D	ARG1436
D	ARG1437
D	GLY1464
D	ARG1465
D	ARG1466
D	HOH2052
D	HOH2057
D	HOH2234
H	HOH2151

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"HAMAP-Rule","id":"MF_04008","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"8805706","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Charge relay system","evidences":[{"source":"HAMAP-Rule","id":"MF_04008","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 8230459, 8805708, 7929296, 12549906, 8805707, 11371196

Chain	Residue	Details
A	ARG165
A	HIS63
A	HIS157
A	SER132

site_id	CSA2
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 8230459, 8805708, 7929296, 12549906, 8805707, 11371196

Chain	Residue	Details
B	ARG465
B	SER432
B	HIS363
B	HIS457

site_id	CSA3
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 8230459, 8805708, 7929296, 12549906, 8805707, 11371196

Chain	Residue	Details
C	HIS1157
C	SER1132
C	ARG1165
C	HIS1063

site_id	CSA4
Number of Residues	4
Details	a catalytic site defined by CSA, PubMed 8230459, 8805708, 7929296, 12549906, 8805707, 11371196

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

246031

PDB entries from 2025-12-10

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