› 1jib

X-ray diffraction
3.3Å resolution

Complex of Alpha-amylase II (TVA II) from Thermoactinomyces vulgaris R-47 with Maltotetraose Based on a Crystal Soaked with Maltohexaose.

Released:
DOI: 10.2210/pdb1jib/pdb
PDB entry 1jib coloured by chain, front view.
PDB entry 1jib coloured by chain, side view.
PDB entry 1jib coloured by chain, top view.
Source organism: Thermoactinomyces vulgaris
Primary publication:
Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.
Yokota T, Tonozuka T, Shimura Y, Ichikawa K, Kamitori S, Sakano Y
Biosci Biotechnol Biochem 65 619-26 (2001)
PMID: 11330677

Function and Biology Details

Reaction catalysed: 
Hydrolysis of pullulan to panose (6-alpha-D-glucosylmaltose)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-170688 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Neopullulanase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 585 amino acids
Theoretical weight: 67.55 KDa
Source organism: Thermoactinomyces vulgaris
Expression system: Escherichia coli
UniProt:
  • Canonical: Q08751 (Residues: 1-585; Coverage: 100%)
Gene name: tvaII
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GLC
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: P212121
Unit cell:
a: 111.87Å b: 117.32Å c: 112.61Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.212 0.212 0.304
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structure and function of α-glucan debranching enzymes.
Møller et al. (2016)
1 more

2 mentions without citation

Defining structural and evolutionary modules in proteins: a community detection approach to explore sub-domain architecture.
Hleap et al. (2013)
1 more