Structure of PDB 4ipm Chain A

Receptor sequence

>4ipmA (length=431) Species: 161573 (Limnoria quadripunctata)

QQAGTETEEYHLPLTWERDGSSVSASVVIDSNWRWTHSTEDTTNCYDGNE
WDSTLCPDADTCTENCAIDGVDQGTWGDTYGITASGSKLTLSFVTEGEYS
TDIGSRVFLMADDDNYEIFNLLDKEFSFDVDASNLPCGLNGALYFVSMDE
DGGTSKYSTNTAGAKYGTGYCDAQCPHDMKFIAGKANSDGWTPSDNDQNA
GTGEMGACCHEMDIWEANSQAQSYTAHVCSVDGYTPCTGTDCGDNGDDRY
KGVCDKDGCDYAAYRLGQHDFYGEGGTVDSGSTLTVITQFITGGGGLNEI
RRIYQQGGQTIQNAAVNFPGDVDPYDSITEDFCVDIKRYFGDTNDFDAKG
GMSGMSNALKKGMVLVMSLWDDHYANMLWLDATYPVDSTEPGALRGPCST
DSGDPADVEANFPGSTVTFSNIKIGPIQSYD

3D structure

• PDB: 4ipm Structural characterization of a unique marine animal family 7 cellobiohydrolase suggests a mechanism of cellulase salt tolerance.
• Chain: A
• Resolution: 1.14 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): E233 D235 E238 H249
• Catalytic site (residue number reindexed from 1): E211 D213 E216 H227
• Enzyme Commision number: 3.2.1.91: cellulose 1,4-beta-cellobiosidase (non-reducing end).

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	SGC	A	R271 D279 Y406 R417	R249 D257 Y384 R395
BS02	BGC	A	H249 D279 W401	H227 D257 W379

Gene Ontology

Molecular Function

• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
• GO:0016162 cellulose 1,4-beta-cellobiosidase activity
• GO:0016798 hydrolase activity, acting on glycosyl bonds

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0030245 cellulose catabolic process

Cellular Component

• GO:0005576 extracellular region

External links

• PDB: RCSB:4ipm, PDBe:4ipm, PDBj:4ipm
• PDBsum: 4ipm
• PubMed: 23733951
• UniProt: D4HRL0|GH7B_LIMQU Exoglucanase GH7B (Gene Name=GH7B)