Research workbench

Barnase mutant with ile 88 replaced by ala

Analyse Barnase mutant with ile 88 replaced by ala in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1BRJ
Type: protein
Length: 322 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Barnase
EC: 3.1.27.-
UniProt: P00648
Ligands: ZN
Pockets: 2 · best druggability 0.57

Structure

x-ray diffraction · 2 distinct chains · 22% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Barnase (EC 3.1.27.-)	protein	108	22% helix, 22% strand	P00648
B, C	Barnase (EC 3.1.27.-)	protein	107	22% helix, 23% strand	P00648

Ligands and binding sites

ZN · Zinc ion · metal · chains C

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	323	0.57	0.76	32	empty
2	54	0.28	0.74	18	empty

Interfaces

2 interfaces between chains.

B–C · 184 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 65 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1BRJ · Barnase mutant with ile 88 replaced by ala · the same entry in another collection · chain A against A, TM-score 1.00

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 1BRJ · PDBe 1BRJ · UniProt P00648

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