Structure of PDB 1pq8 Chain A

Receptor sequence
>1pq8A (length=224) Species: 5507 (Fusarium oxysporum) [Search protein sequence]
IVGGTSASAGDFPFIVSISRNGGPWCGGSLLNANTVLTAAHCVSGYAQSG
FQIRAGSLSRTSGGITSSLSSVRVHPSYSGNNNDLAILKLSTSIPSGGNI
GYARLAASGSDPVAGSSATVAGWGATSEGGSSTPVNLLKVTVPIVSRATC
RAQYGTSAITNQMFCAGVSSGGKDSCQGDSGGPIVDSSNTLIGAVSWGNG
CARPNYSGVYASVGALRSFIDTYA
3D structure
PDB1pq8 Trypsin Revisited: CRYSTALLOGRAPHY AT (SUB) ATOMIC RESOLUTION AND QUANTUM CHEMISTRY REVEALING DETAILS OF CATALYSIS.
ChainA
Resolution1.0 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) H56 D99 Q192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H41 D84 Q177 G178 D179 S180 G181
Enzyme Commision number 3.4.21.4: trypsin.
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 H56 N96 D189 S190 C191 Q192 G193 S195 S211 W212 H41 N81 D174 S175 C176 Q177 G178 S180 S196 W197
BS02 LYS A H56 C191 Q192 S195 S211 W212 G213 G215 H41 C176 Q177 S180 S196 W197 G198 G200
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005576 extracellular region

View graph for
Molecular Function

View graph for
Biological Process

View graph for
Cellular Component
External links
PDB RCSB:1pq8, PDBe:1pq8, PDBj:1pq8
PDBsum1pq8
PubMed12937176
UniProtP35049|TRYP_FUSOX Trypsin

[Back to BioLiP]