› 2x2y

X-ray diffraction
2.35Å resolution

Cellulomonas fimi endo-beta-1,4-mannanase double mutant

Released:
DOI: 10.2210/pdb2x2y/pdb
Model geometry
Fit model/data
PDB entry 2x2y coloured by chain, front view.
PDB entry 2x2y coloured by chain, side view.
PDB entry 2x2y coloured by chain, top view.
Source organism: Cellulomonas fimi
Primary publication:
Rational engineering of mannosyl binding in the distal glycone subsites of Cellulomonas fimi endo-beta-1,4-mannanase: mannosyl binding promoted at subsite -2 and demoted at subsite -3.
Hekmat O, Lo Leggio L, Rosengren A, Kamarauskaite J, Kolenova K, Stålbrand H
Biochemistry 49 4884-96 (2010)
PMID: 20426480

Function and Biology Details

Reaction catalysed: 
Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194995 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Man26A Chains: A, B
Molecule details ›
Chains: A, B
Length: 475 amino acids
Theoretical weight: 50.47 KDa
Source organism: Cellulomonas fimi
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9XCV5 (Residues: 52-514; Coverage: 48%)
Gene name: man26A
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand FMT 8 x FMT
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: MAX II BEAMLINE I911-2
Spacegroup: P212121
Unit cell:
a: 73.093Å b: 99.555Å c: 132.97Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.16 0.158 0.199
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Production, properties, and applications of endo-β-mannanases.
Srivastava et al. (2017)
2 more

4 mentions without citation

Structure of LdtMt2, an L,D-transpeptidase from Mycobacterium tuberculosis.
Böth et al. (2013)
3 more