1BGS: Barnase

Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar. Determined by X-ray diffraction at 2.6 Å resolution. Released 30 Apr 1994.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Bacillus amyloliquefaciens
Chains: 6
Atoms: 4,987
Mol. weight: 67.67 kDa
Released: 30 Apr 1994

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

Secondary structure: helices and β-sheets

1BGS contains 22 α-helices and 30 β-strands across 6 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: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	7-17	11
β-strand	24-25	2	1
α-helix	27-33	7
α-helix	42-45	4
β-strand	50-51	2	1
β-strand	52-56	5	2
β-strand	71-75	5	2
β-strand	87-91	5	2
β-strand	96-99	4	2
β-strand	107-108	2	2

Chain B: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	7-17	11
β-strand	24-25	2	3
α-helix	27-31	5
α-helix	42-45	4
β-strand	50-51	2	3
β-strand	52-56	5	4
β-strand	71-75	5	4
β-strand	87-91	5	4
β-strand	96-99	4	4
β-strand	107-108	2	4

Chain C: 3 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	7-17	11
β-strand	24-25	2	5
α-helix	27-32	6
α-helix	42-45	4
β-strand	50-51	2	5
β-strand	52-56	5	6
β-strand	71-75	5	6
β-strand	87-91	5	6
β-strand	96-99	4	6
β-strand	107-108	2	6

Chains E and G: 4 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	7
α-helix	13-24	12
α-helix	34-43	10
β-strand	49-54	6	7
α-helix	56-62	7
α-helix	67-79	13
β-strand	84-88	5	7

Chain F: 5 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	2-6	5	8
α-helix	7-9	3
α-helix	13-24	12
α-helix	34-43	10
β-strand	49-54	6	8
α-helix	56-62	7
α-helix	66-79	14
β-strand	84-88	5	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Barnase	A, B, C	protein	110	Bacillus amyloliquefaciens	P00648 (AlphaFold model)
Barstar	E, F, G	protein	89	Bacillus amyloliquefaciens	P11540 (AlphaFold model)

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

>1BGS_1 BARNASE (chains A, B, C)
AQVINTFDGVADYLQTYHKLPDNYITKSEAQALGWVASKGNLADVAPGKSIGGDIFSNRE
GKLPGKSGRTWREADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR

Sequence of entity 2 (E, F, G), FASTA

>1BGS_2 BARSTAR (chains E, F, G)
KKAVINGEQIRSISDLHQTLKKELALPEYYGENLDALWDALTGWVEYPLVLEWRQFEQSK
QLTENGAESVLQVFREAKAEGADITIILS

Primary citation

Recognition between a bacterial ribonuclease, barnase, and its natural inhibitor, barstar. Guillet, V., Lapthorn, A., Hartley, R.W. et al. Structure (1993) 1:165-176. DOI 10.1016/0969-2126(93)90018-C · 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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