Structure of PDB 4bnr Chain B

Receptor sequence
>4bnrB (length=237) Species: 6717 (Astacus leptodactylus) [Search protein sequence]
IVGGTDATLGEFPYQLSFQETFIGFSFHFCGASIYNENYAITAGHCVYGD
DYENPSGLQIVAGELDMSVNEGSEQIITVSKIILHENFDYNLLDNDISLL
KLSGSLTFNDNVAPIALPEQGHTATGDVIVTGWGTTSEGGNTPDVLQKVT
VPLVSDEDCRADYGADEILDSMICAGVPEGGKDSCQGDSGGPLAASDTGS
TYLAGIVSWGYGCARPGYPGVYTEVSYHVDWIKANAV
3D structure
PDB4bnr Comparison of Complexes Formed by a Crustacean and a Vertebrate Trypsin with Bovine Pancreatic Trypsin Inhibitor - the Key to Achieving Extreme Stability?
ChainB
Resolution2.0 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) H45 D96 Q186 G187 D188 S189 G190
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 B E70 D72 V75 E77 E80 E64 D66 V69 E71 E74
BS02 CA B D165 D178 M180 E231 D156 D170 M172 E224
Gene Ontology
Molecular Function
GO:0004252 serine-type endopeptidase activity
GO:0005515 protein binding
GO:0008236 serine-type peptidase activity
GO:0046872 metal ion binding
Biological Process
GO:0006508 proteolysis

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Molecular Function
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Biological Process
External links
PDB RCSB:4bnr, PDBe:4bnr, PDBj:4bnr
PDBsum4bnr
PubMed24034223
UniProtQ52V24

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