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Cross-linked barnase soaked in 3 M thiourea

Analyse Cross-linked barnase soaked in 3 M thiourea in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2F5W
Type: protein
Length: 324 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ribonuclease
EC: 3.1.27.-
UniProt: P00648
Ligands: TOU, ZN
Pockets: 1 · best druggability 0.54

Structure

x-ray diffraction · 1 distinct chain · 22% helix, 23% strand (DSSP).

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

Ligands and binding sites

TOU · Thiourea · ligand · chains C
ZN · Zinc ion · metal · chains C

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	352	0.54	0.74	31	empty

Interfaces

3 interfaces between chains.

B–C · 204 Å² buried · 4 hydrogen bonds · protein-protein
A–C · 31 Å² buried · 0 hydrogen bonds · protein-protein
A–B · 17 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

2F5W · Cross-linked barnase soaked in 3 M thiourea · 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 2F5W · PDBe 2F5W · UniProt P00648

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