Structure of PDB 3vt2 Chain F

Receptor sequence
>3vt2F (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
ChainF
Resolution3.002 Å
3D
structure
Catalytic site residues are labeled in the 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
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 F D416 K418 D419 E420 Y431 N434 D384 K386 D387 E388 Y399 N402
BS02 IPT F E112 Y137 D180 N200 E229 G249 W250 Q282 E80 Y105 D148 N168 E197 G217 W218 Q250
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

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

[Back to BioLiP]