Research workbench

Cyanovirin-N mutation I34Y with dimannose bound

Analyse Cyanovirin-N mutation I34Y with dimannose bound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6X7H
Type: protein
Length: 200 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyanovirin-N
UniProt: P81180
Ligands: MAN
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 2 distinct chains · 13% helix, 57% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cyanovirin-N	protein	100	12% helix, 58% strand	P81180
B	Cyanovirin-N	protein	100	13% helix, 56% strand	P81180

Ligands and binding sites

MAN · alpha-D-mannopyranose · sugar · 4 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	90	0.34	0.74	15	MAN

Interfaces

1 interface between chains.

A–B · 475 Å² buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

6X7H · Cyanovirin-N Mutation I34Y with Dimannose bound · the same entry in another collection · chain A against A, TM-score 1.00
P81180 · AlphaFold monomer V2.0 prediction for cyanovirin-N (P81180) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P81180
Elsewhere: RCSB PDB 6X7H · PDBe 6X7H · UniProt P81180

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