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The contribution of buried hydrogen bonds to protein stability: the crystal structures of two barnase mutants

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PDB: 1BAN
Type: protein
Length: 325 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Barnase
EC: 3.1.27.-
UniProt: P00648
Pockets: 2 · best druggability 0.44

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Barnase (EC 3.1.27.-)	protein	108	22% helix, 23% strand	P00648
C	Barnase (EC 3.1.27.-)	protein	109	21% helix, 25% strand	P00648

Pockets

2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	198	0.44	0.73	26	empty
2	51	0.26	0.73	18	empty

Interfaces

2 interfaces between chains.

B–C · 193 Å² buried · 3 hydrogen bonds · protein-protein
A–B · 18 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1BAN · The contribution of buried hydrogen bonds to protein stability: the crystal structures of… · the same entry in another collection · chain A against A, TM-score 1.00
P00648 · AlphaFold monomer V2.0 prediction for ribonuclease (P00648) · a predicted model of the same protein · chain A against A, TM-score 0.99

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00648
Elsewhere: RCSB PDB 1BAN · PDBe 1BAN · UniProt P00648

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