Structure of PDB 3qho Chain C

Receptor sequence
>3qhoC (length=377) Species: 53953 (Pyrococcus horikoshii) [Search protein sequence]
QTPTGIYYEVRGDTIYMINVTSGEETPIHLFGVNWFGFETPNHVVHGLWK
RNWEDMLLQIKSLGFNAIRLPFCTESVKPGTQPIGIDYSKNPDLRGLDSL
QIMEKIIKKAGDLGIFVLLDYHRIGCTHIEPLWYTEDFSEEDFINTWIEV
AKRFGKYWNVIGADLKNEPHSVTSPPAAYTDGTGATWGMGNPATDWNLAA
ERIGKAILKVAPHWLIFVEGTQFTNPKTDSSYKWGYNAWWGGNLMAVKDY
PVNLPRNKLVYSPHVFGPDVYNQPYFGPAKGFPDNLPDIWYHHFGYVKLE
LGYSVVIGEFGGKYGHGGDPRDVIWQNKLVDWMIENKFCDFFYWSWNPDS
GDTGGILQDDWTTIWEDKYNNLKRLMD
3D structure
PDB3qho Functional analysis of hyperthermophilic endocellulase from Pyrococcus horikoshii by crystallographic snapshots
ChainC
Resolution1.65 Å
3D
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
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 W273 Q222 A238 W239 W240
BS02 BGC C E201 W272 W273 F299 E168 W239 W240 F266
BS03 BGC C H155 E201 F299 E342 W377 D385 H122 E168 F266 E309 W344 D352
BS04 BGC C F69 E72 S383 F36 E39 S350
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

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:3qho, PDBe:3qho, PDBj:3qho
PDBsum3qho
PubMed21557724
UniProtO58925

[Back to BioLiP]