Structure of PDB 1at3 Chain A

Receptor sequence
>1at3A (length=217) Species: 10310 (Human alphaherpesvirus 2) [Search protein sequence]
RAVPIYVAGFLALYDSGDPGELALDPDTVRAALPPENPLPINVDHRARCE
VGRVLAVVNDPRGPFFVGLIACVQLERVLETAASAAILSREERLLYLITN
YLPSVSLSTKPDRTLFAHVALCAIGRRLGTIVTYDTSLDAAIAPFRHLDP
ATREGVRREAAEAELALAGRTWAPGVEALTHTLLSTAVNNMMLRDRWSLV
AERRRQAGIAGHTYLQA
3D structure
PDB1at3 Active site cavity of herpesvirus proteases revealed by the crystal structure of herpes simplex virus protease/inhibitor complex.
ChainA
Resolution2.5 Å
3D
structure
Catalytic site residues are labeled in the structure
[Spin on]
[Spin off]
[Reset orientation]

[High quality]
[Low quality]

[White background]
[Black background]

[Download]
[Download structure with residue number starting from 1]
Enzymatic activity
Catalytic site (original residue number in PDB) H61 S129 S131 H148 R156 R157
Catalytic site (residue number reindexed from 1) H45 S106 S108 H118 R126 R127
Enzyme Commision number 3.4.21.97: assemblin.
Interaction with ligand
Site
#
Ligand Ligand
chain
Binding residues on receptor
(original residue number in PDB)
Binding residues on receptor
(residue number reindexed from 1)
Binding affinity
BS01 DFP A H61 S129 L130 C152 R156 H45 S106 L107 C122 R126
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:1at3, PDBe:1at3, PDBj:1at3
PDBsum1at3
PubMed9369473
UniProtQ69527

[Back to BioLiP]