1B2U: Protein
Structural response to mutation at a protein-protein interface. Determined by X-ray diffraction at 2.1 Å resolution. Released 9 Dec 1998.
- Method
- X-ray diffraction
- Resolution
- 2.1 Å
- Organism
- Bacillus amyloliquefaciens
- Chains
- 6
- Atoms
- 5,111
- Mol. weight
- 67.95 kDa
- Released
- 9 Dec 1998
Explore 1B2U in 3D
Show helices and sheets
RCSB PDB
PDBe
Secondary structure: helices and β-sheets
1B2U contains 24 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: 4 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-17 | 11 | |
| β-strand | 24-25 | 2 | 1 |
| α-helix | 27-32 | 6 | |
| α-helix | 37-39 | 3 | |
| 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 | 27-32 | 6 | |
| 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: 4 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| α-helix | 7-17 | 11 | |
| β-strand | 24-25 | 2 | 5 |
| α-helix | 27-33 | 7 | |
| α-helix | 37-39 | 3 | |
| 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 |
Chain D: 5 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 2-7 | 6 | 7 |
| α-helix | 8-10 | 3 | |
| α-helix | 14-24 | 11 | |
| α-helix | 35-44 | 10 | |
| β-strand | 50-55 | 6 | 7 |
| α-helix | 57-62 | 6 | |
| α-helix | 67-80 | 14 | |
| β-strand | 85-89 | 5 | 7 |
Chain E: 3 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 4-7 | 4 | 8 |
| α-helix | 14-25 | 12 | |
| α-helix | 35-44 | 10 | |
| β-strand | 50-55 | 6 | 8 |
| α-helix | 68-81 | 14 | |
| β-strand | 85-89 | 5 | 8 |
Chain F: 5 helices, 3 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 3-7 | 5 | 9 |
| α-helix | 8-10 | 3 | |
| α-helix | 14-24 | 11 | |
| α-helix | 35-44 | 10 | |
| β-strand | 50-55 | 6 | 9 |
| α-helix | 57-62 | 6 | |
| α-helix | 67-81 | 15 | |
| β-strand | 85-89 | 5 | 9 |
Molecules and chains
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|
| Protein (barnase) | A, B, C | protein | 110 | Bacillus amyloliquefaciens | P00648 (AlphaFold model) |
| Protein (barstar) | D, E, F | protein | 90 | Bacillus amyloliquefaciens | P11540 (AlphaFold model) |
Sequence of entity 1 (A, B, C), FASTA
>1B2U_1 PROTEIN (BARNASE) (chains A, B, C)
AQVINTFDGVADYLQTYHKLPDNYITASEAQALGWVASKGNLADVAPGKSIGGDIFSNRE
GKLPGKSGRTWREADINYTSGFRNSDRILYSSDWLIYKTTDHYQTFTKIR
Sequence of entity 2 (D, E, F), FASTA
>1B2U_2 PROTEIN (BARSTAR) (chains D, E, F)
MKKAVINGEQIRSISDLHQTLKKELALPEYYGENLAALWDCLTGWVEYPLVLEWRQFEQS
KQLTENGAESVLQVFREAKAEGCDITIILS
Primary citation
Structural response to mutation at a protein-protein interface. Vaughan, C.K., Buckle, A.M., Fersht, A.R. J Mol Biol (1999) 286:1487-1506. DOI 10.1006/jmbi.1998.2559 · 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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