Structure of PDB 3qhn Chain B

Receptor sequence
>3qhnB (length=377) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]
QTPTGIYYEVRGDTIYMINVTSGEETPIHLFGVNWFGFETPNHVVHGLWK
RNWEDMLLQIKSLGFNAIRLPFCTESVKPGTQPIGIDYSKNPDLRGLDSL
QIMEKIIKKAGDLGIFVLLDYHRIGCTHIEPLWYTEDFSEEDFINTWIEV
AKRFGKYWNVIGADLKNAPHSVTSPPAAYTDGTGATWGMGNPATDWNLAA
ERIGKAILKVAPHWLIFVEGTQFTNPKTDSSYKWGYNAWWGGNLMAVKDY
PVNLPRNKLVYSPHVYGPDVYNQPYFGPAKGFPDNLPDIWYHHFGYVKLE
LGYSVVIGEFGGKYGHGGDPRDVIWQNKLVDWMIENKFCDFFYWSWNPDS
GDTGGILQDDWTTIWEDKYNNLKRLMD
3D structure
PDB3qhn Functional analysis of hyperthermophilic endocellulase from Pyrococcus horikoshii by crystallographic snapshots
ChainB
Resolution1.99 Å
3D
structure
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Enzymatic activity
Enzyme Commision number 3.2.1.4: cellulase.
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 BGC B A271 W272 W273 A238 W239 W240
BS02 BGC B W272 W273 Y299 W239 W240 Y266
BS03 BGC B Y299 E342 W377 D385 Y266 E309 W344 D352
BS04 BGC B F69 E72 S383 G384 F36 E39 S350 G351
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
GO:0016798 hydrolase activity, acting on glycosyl bonds
GO:0046872 metal ion binding
Biological Process
GO:0000272 polysaccharide catabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3qhn, PDBe:3qhn, PDBj:3qhn
PDBsum3qhn
PubMed21557724
UniProtO58925

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