1BRH: Barnase mutant with leu 14 replaced by ala

Barnase mutant with leu 14 replaced by ala. Determined by X-ray diffraction at 2.0 Å resolution. Released 10 Jul 1995.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Bacillus amyloliquefaciens
Chains
3
Atoms
2,802
Mol. weight
37.14 kDa
Ligands
ZN
Released
10 Jul 1995

Explore 1BRH in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1BRH contains 13 α-helices and 21 β-strands across 3 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 5 helices, 7 β-strands

ElementResiduesLengthSheet
α-helix7-1711
β-strand24-2521
α-helix27-326
α-helix37-393
α-helix42-454
β-strand50-5121
β-strand52-5652
α-helix64-652
β-strand71-7552
β-strand87-9152
β-strand96-9942
β-strand107-10822
Chains B and C: 4 helices, 7 β-strands
ElementResiduesLengthSheet
α-helix7-1711
β-strand24-2523
α-helix27-326
α-helix37-393
α-helix42-454
β-strand50-5123
β-strand52-5654
β-strand71-7554
β-strand87-9154
β-strand96-9944
β-strand107-10824

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
BarnaseA, B, Cprotein110Bacillus amyloliquefaciensP00648 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>1BRH_1 BARNASE (chains A, B, C)
AQVINTFDGVADYAQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNRE
GKLPGKSGRTWREADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn1

Primary citation

Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Buckle, A.M., Cramer, P., Fersht, A.R. Biochemistry (1996) 35:4298-4305. DOI 10.1021/bi9524676 · PubMed

Other PDB entries of the same protein (UniProt P00648 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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