Structure of PDB 3qhm Chain C

Receptor sequence
>3qhmC (length=377) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]
QTPTGIYYEVRGDTIYMINVTSGEETPIHLFGVNWFGFETPNHVVHGLWK
RNWEDMLLQIKSLGFNAIRLPFCTESVKPGTQPIGIDYSKNPDLRGLDSL
QIMEKIIKKAGDLGIFVLLDYHRIGCTHIEPLWYTEDFSEEDFINTWIEV
AKRFGKYWNVIGADLKNEPHSVTSPPAAYTDGTGATWGMGNPATDWNLAA
ERIGKAILKVAPHWLIFVEGTQFTNPKTDSSYKWGYNAWWGGNLMAVKDY
PVNLPRNKLVYSPHVYGPDVYNQPYFGPAKGFPDNLPDIWYHHFGYVKLE
LGYSVVIGAFGGKYGHGGDPRDVIWQNKLVDWMIENKFCDFFYWSWNPDS
GDTGGILQDDWTTIWEDKYNNLKRLMD
3D structure
PDB3qhm Functional analysis of hyperthermophilic endocellulase from Pyrococcus horikoshii by crystallographic snapshots
ChainC
Resolution2.01 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 C Q255 A271 W272 Y304 Q222 A238 W239 Y271
BS02 BGC C H155 E201 Y299 V303 W377 D385 H122 E168 Y266 V270 W344 D352
BS03 BGC C F69 E72 R156 F36 E39 R123
BS04 BGC C H79 D382 G384 H46 D349 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
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3qhm, PDBe:3qhm, PDBj:3qhm
PDBsum3qhm
PubMed21557724
UniProtO58925

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