MolNFT v1 · #180203 · protein

Crystal structure on act C 10.0101

7KSB · Non-specific lipid-transfer protein 1: “Crystal structure on act C 10.0101”. X-ray diffraction, 1 ligand (SO4), 1 pocket (best druggability 0.33). MolNFT v1 #180203 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 7KSB
Type: protein
Length: 184 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Non-specific lipid-transfer protein 1
UniProt: P85204
Ligands: SO4
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Non-specific lipid-transfer protein 1	protein	92	64% helix, 0% strand	P85204

Ligands and binding sites

SO4 · Sulfate ion · ion · 6 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	72	0.33	0.76	22	empty

Interfaces

1 interface between chains.

A–B · 631 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 disulfide (disulfide).

Compared structures

7KSB · Crystal structure on Act c 10.0101 · the same entry in another collection · chain A against A, TM-score 1.00
P85204 · AlphaFold monomer V2.0 prediction for non-specific lipid-transfer protein 1 (P85204) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P85204
Elsewhere: RCSB PDB 7KSB · PDBe 7KSB · UniProt P85204

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