Structure of PDB 3vt2 Chain A

Receptor sequence
>3vt2A (length=461) Species: 203119 (Acetivibrio thermocellus ATCC 27405) [Search protein sequence]
EGVIVNGTQFKDTSGNVIHAHGGGMLKHGDYYYWYGEYRDDSNLFLGVSC
YRSKDLVNWEYRGEVLSRNSAPELNHCNIERPKVMYNASTGEFVMWMHWE
NGINYGQARAAVAYSKTPDGKFTYIRSFRPMQDTGVMDHGLPGYMSRDCN
VFVDTDGKGYFISAANENMDLHLYELTPDYKNIASLKAKLFVGQQREAPC
LIKRNGYYYLITSGCTGWNPNQAKYAYSKDLASGWSQLYNLGNSTTYRSQ
PTFIIPVQGSSGTSYLYMGDRWAGAWGGKVNDSQYVWLPLNFISDTTLEL
PYYDSVKIDASSGIISEYIPDTTRYKLVNKNSGKVLDVLDGSVDNAAQIV
QWTDNGSLSQQWYLVDVGGGYKKIVNVKSGRALDVKDESKEDGGVLIQYT
SNGGYNQHWKFTDIGDGYYKISSRHCGKLIDVRKWSTEDGGIIQQWSDAG
GTNQHWKLVLV
3D structure
PDB3vt2 Crystal structure of 1,3Gal43A, an exo-beta-1,3-galactanase from Clostridium thermocellum
ChainA
Resolution3.002 Å
3D
structure
Catalytic site residues are labeled in the structure
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Enzymatic activity
Catalytic site (original residue number in PDB) T45
Catalytic site (residue number reindexed from 1) T13
Enzyme Commision number ?
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 IPT A D416 D419 E420 Y431 N434 N438 D384 D387 E388 Y399 N402 N406
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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Molecular Function
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Biological Process
External links
PDB RCSB:3vt2, PDBe:3vt2, PDBj:3vt2
PDBsum3vt2
PubMed22960181
UniProtA3DD67

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