Structure of PDB 1mbq Chain A

Receptor sequence
>1mbqA (length=220) Species: 8018 (Oncorhynchus keta) [Search protein sequence]
IVGGYECKAYSQPHQVSLNSGYHFCGGSLVNENWVVSAAHCYKSRVEVRL
GEHNIKVTEGSEQFISSSRVIRHPNYSSYNIDNDIMLIKLSKSATLNTYV
QPVALPSSCAPAGTMCTVSGWGNTMSSTADKNKLQCLNIPILSYSDCNNS
YPGMITNAMFCAGYLEGGKDSCQGDSGGPVVCNGELQGVVSWGYGCAEPG
NPGVYAKVCIFNDWLTSTMA
3D structure
PDB1mbq Crystal Structure and Nucleotide Sequence of an Anionic Trypsin from Chum Salmon (Oncorhynchus keta) in Comparison with Atlantic Salmon (Salmo salar) and Bovine Trypsin
ChainA
Resolution1.8 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) H57 D102 Q192 G193 D194 S195 G196
Catalytic site (residue number reindexed from 1) H40 D84 Q173 G174 D175 S176 G177
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 E70 N72 V75 E77 E80 E52 N54 V57 E59 E62
BS02 BEN A D189 S190 C191 S195 V213 W215 G219 D170 S171 C172 S176 V190 W192 G195
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis
Cellular Component
GO:0005576 extracellular region
GO:0005615 extracellular space

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Biological Process
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Cellular Component
External links
PDB RCSB:1mbq, PDBe:1mbq, PDBj:1mbq
PDBsum1mbq
PubMed12445776
UniProtQ8AV11

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