Structure of PDB 2fmj Chain A

Receptor sequence
>2fmjA (length=222) Species: 1911 (Streptomyces griseus) [Search protein sequence]
VVGGTRAAQGEFPFMVRLSMGCGGALYAQDIVLTAAHCVSGSGNNTSITA
TGGVVDLQSSSAVKVRSTKVLQAPGYNGTGKDWALIKLAQPINQPTLKIA
TTTAYNQGTFTVAGWGANREGGSQQRYLLKANVPFVSDAACRSAYGNELV
ANEEICAGYDTGGVDTCQGDSGGPMFRKDNADEWIQVGIVSWGEGCARKG
KYGVYTEVSTFASAIASAARTL
3D structure
PDB2fmj Conversion of trypsin into a Na(+)-activated enzyme.
ChainA
Resolution1.65 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) H57 D102 Q192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H37 D82 Q168 G169 D170 S171 G172
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 CA A D165 A177A E180 E230 D138 A151 E154 E207
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
Biological Process
GO:0006508 proteolysis

View graph for
Molecular Function

View graph for
Biological Process
External links
PDB RCSB:2fmj, PDBe:2fmj, PDBj:2fmj
PDBsum2fmj
PubMed16503653
UniProtP00775|TRYP_STRGR Trypsin (Gene Name=sprT)

[Back to BioLiP]