Structure of PDB 2vr5 Chain A

Receptor sequence

>2vr5A (length=715) Species: 2287 (Saccharolobus solfataricus)

FFRTRDRPLRPGDPYPLGSNWIEDDDGVNFSLFSENAEKVELLLYSLTNQ
KYPKEIIEVKNKTGDIWHVFVPGLRPGQLYAYRVYGPYKPELGLRFNPNK
VLIDPYAKAINGSVIWNDAVFGYKIGDQNQDLTYDERDSGEYVPKSVVIN
PYFEWDDEDFIKGKKVPLKDTVIYEVHVKGFTKLRLDLPENIRGTYEGLA
SEQMISYLKDLGITTVELMPVFHFIDQRFLTDKGLTNYWGYDPINFFSPE
CRYSSTGCLGGQVLSFKKMVNELHNAGIEVIIDVVYNHTAEGNHLGPTLS
FRGIDNTAYYMLQPDNKRYYLDFTGTGNTLNLSHPRVIQMVLDSLRYWVT
EMHVDGFRFDLAAALARELYSVNMLNTFFIALQQDPILSQVKLIAEPWDV
GQGGYQVGNFPYQWAEWNGKYRDSIRRFWRGEALPYSEIANRLLGSPDIY
LGNNKTPFASINYVTSHDGFTLEDLVSYNQKHNEANGFNNQDGMNENYSW
NCGAEGPTNDQNVVICREKQKRNFMITLLVSQGTPMILGGDELSRTQRGN
NNAFCQDNEITWFDWNLDERKSKFLEFVKKMIQFYRAHPAFRRERYFQGK
KLFGMPLKDVTFYTLEGREVDEKTWSSPTQLVIFVLEGSVMDEINMYGER
IADDSFLIILNANPNNVKVKFPKGKWELVISSYLREIKPEERIIEGEKEL
EIEGRTALVYRRIEL

3D structure

• PDB: 2vr5 Structural Insight Into the Bifunctional Mechanism of the Glycogen-Debranching Enzyme Trex from the Archaeon Sulfolobus Solfataricus.
• Chain: A
• Resolution: 2.8 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): S116 H226 F227 E253 D363 E399 D471
• Catalytic site (residue number reindexed from 1): S113 H223 F224 E250 D360 E396 D468
• Enzyme Commision number: 3.2.1.-

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	GLC	A	Y408 K423	Y405 K420
BS02	GLC	A	W401 V403 Y408	W398 V400 Y405
BS03	A16	A	W242 Y244 H291 D363 H470 D471 D495	W239 Y241 H288 D360 H467 D468 D492

Gene Ontology

Molecular Function

• GO:0004133 glycogen debranching enzyme activity
• GO:0004177 aminopeptidase activity
• GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds

Biological Process

• GO:0005975 carbohydrate metabolic process
• GO:0005980 glycogen catabolic process

External links

• PDB: RCSB:2vr5, PDBe:2vr5, PDBj:2vr5
• PDBsum: 2vr5
• PubMed: 18703518
• UniProt: P95868