Structure of PDB 1nln Chain A

Receptor sequence
>1nlnA (length=203) Species: 10515 (Human adenovirus 2) [Search protein sequence]
GSSEQELKAIVKDLGCGPYFLGTYDKRFPGFVSPHKLACAIVNTAGRETG
GVHWMAFAWNPRSKTCYLFEPFGFSDQRLKQVYQFEYESLLRRSAIASSP
DRCITLEKSTQSVQGPNSAACGLFCCMFLHAFANWPQTPMDHNPTMNLIT
GVPNSMLNSPQVQPTLRRNQEQLYSFLERHSPYFRSHSAQIRSATSFCHL
KNM
3D structure
PDB1nln Crystallographic structure at 1.6-A resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor: insights on a new fold
ChainA
Resolution1.6 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) H54 E71 Q115 C122
Catalytic site (residue number reindexed from 1) H53 E70 Q114 C121
Enzyme Commision number 3.4.22.39: adenain.
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 peptide A D77 E89 R93 R103 C104 I105 T106 L107 E108 K109 S110 T111 Q112 M141 D142 M147 I150 D76 E88 R92 R102 C103 I104 T105 L106 E107 K108 S109 T110 Q111 M140 D141 M146 I149
Gene Ontology
Molecular Function
GO:0003677 DNA binding
GO:0004197 cysteine-type endopeptidase activity
GO:0008234 cysteine-type peptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0042025 host cell nucleus
GO:0044423 virion component

View graph for
Molecular Function
View graph for
Biological Process
View graph for
Cellular Component
External links
PDB RCSB:1nln, PDBe:1nln, PDBj:1nln
PDBsum1nln
PubMed12758141
UniProtP03252|PRO_ADE02 Protease (Gene Name=L3)

[Back to BioLiP]