MolNFT v1 · #124169 · protein

Structure and anti-HIV activity of cyt-cvnh, a new cyanovirin-N homolog

5K79 · Cyanovirin-N domain protein: “Structure and anti-HIV activity of cyt-cvnh, a new cyanovirin-N homolog”. X-ray diffraction, 1 pocket (best druggability 0.33). MolNFT v1 #124169 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 5K79
Type: protein
Length: 216 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyanovirin-N domain protein
UniProt: B7KDN5
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 56% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cyanovirin-N domain protein	protein	108	11% helix, 56% strand	B7KDN5

Ligands and binding sites

PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · chains 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	66	0.33	0.76	19	empty

Interfaces

1 interface between chains.

A–B · 695 Å² buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

5K79 · Structure and anti-HIV activity of CYT-CVNH, a new cyanovirin-n homolog · 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 B7KDN5
Elsewhere: RCSB PDB 5K79 · PDBe 5K79 · UniProt B7KDN5

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