2F5M: Cross-linked barnase soaked in bromo-ethanol

Cross-linked barnase soaked in bromo-ethanol. Determined by X-ray diffraction at 1.95 Å resolution. Released 25 Apr 2006.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Bacillus amyloliquefaciens
Chains: 3
Atoms: 2,805
Mol. weight: 36.85 kDa
Ligands: BRJ
Released: 25 Apr 2006

Explore 2F5M in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2F5M contains 14 α-helices and 23 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

Element	Residues	Length	Sheet
α-helix	5-15	11
β-strand	22-23	2	1
α-helix	25-30	6
α-helix	35-37	3
α-helix	40-43	4
β-strand	48-49	2	1
β-strand	50-54	5	2
α-helix	62-63	2
β-strand	69-73	5	2
β-strand	85-89	5	2
β-strand	94-97	4	2
β-strand	105-106	2	2

Chain B: 5 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
β-strand	22-23	2	3
α-helix	25-30	6
α-helix	35-37	3
β-strand	39	1	4
α-helix	40-43	4
β-strand	48-49	2	3
β-strand	50-54	5	5
α-helix	62-63	2
β-strand	69-73	5	5
β-strand	79	1	4
β-strand	85-89	5	5
β-strand	94-97	4	5
β-strand	105-106	2	5

Chain C: 4 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	5-15	11
β-strand	22-23	2	6
α-helix	25-30	6
α-helix	35-37	3
α-helix	40-43	4
β-strand	48-49	2	6
β-strand	50-54	5	7
β-strand	69-73	5	7
β-strand	85-89	5	7
β-strand	94-97	4	7
β-strand	105-106	2	7

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ribonuclease	A, B, C	protein	108	Bacillus amyloliquefaciens	P00648 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>2F5M_1 Ribonuclease (chains A, B, C)
VINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNREGK
LPGKSGRTWREADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR

Ligands and cofactors

ID	Name	Formula	Copies
BRJ	2-bromoethanol	C2 H5 Br O	2

Primary citation

On the edge of the denaturation process: Application of X-ray diffraction to barnase and lysozyme cross-linked crystals with denaturants in molar concentrations. Salem, M., Mauguen, Y., Prange, T. Biochim Biophys Acta (2006) 1764:903-912. DOI 10.1016/j.bbapap.2006.02.009 · PubMed

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

6PQK 1.2 Å, Cryogenic crystal structure of barnase A43C/S80C bound to barstar C40A/S59C/A67C/C82A
2C4B 1.3 Å, Inhibitor cystine knot protein McoEeTI fused to the catalytically inactive barnase…
1A2P 1.5 Å, Barnase wildtype structure at 1.5 Å resolution
2ZA4 1.58 Å, Crystal Structural Analysis of Barnase-barstar Complex
1B20 1.7 Å, Deletion of a buried salt-bridge in barnase
1BRN 1.76 Å, Subsite binding in an RNase: structure of a barnase-tetranucleotide complex at 1.76 Å…
1B2X 1.8 Å, Barnase wildtype structure at PH 7.5 from a cryo_cooled crystal at 100K
1B2S 1.82 Å, Structural response to mutation at a protein-protein interface
1BRI 1.9 Å, Barnase mutant with ile 76 replaced by ala
1RNB 1.9 Å, Crystal structure of a barnase-d(*gp*c) complex at 1.9 Å resolution
1X1Y 1.9 Å, Water-mediate interaction at aprotein-protein interface
3KCH 1.94 Å, Baranase crosslinked by glutaraldehyde

Browse structure collections

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