MolNFT v1 · #112270 · protein

Crystal structure analysis of kelch protein (with disulfide bond) from plasmodium falciparum

4ZGC: “Crystal structure analysis of kelch protein (with disulfide bond) from plasmodium falciparum”. X-ray diffraction, 1 ligand (UNX), 9 pockets (best druggability 0.79). MolNFT v1 #112270 on GenesisL1: 3D structure, binding sites and…

PDB: 4ZGC
Type: protein
Length: 745 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Kelch protein
UniProt: A0A077LQB4
Ligands: UNX
Pockets: 9 · best druggability 0.79

Structure

x-ray diffraction · 2 distinct chains · 10% helix, 40% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Kelch protein	protein	372	10% helix, 39% strand	A0A077LQB4
B	Kelch protein	protein	373	10% helix, 41% strand	A0A077LQB4

Ligands and binding sites

UNX · Unknown atom or ion · ion · 36 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1040	0.79	0.81	89	UNX
2	514	0.77	0.85	41	empty
3	125	0.46	0.78	31	UNX
4	108	0.46	0.79	23	UNX
5	59	0.45	0.84	17	UNX

Interfaces

1 interface between chains.

A–B · 1282 Å² buried · 16 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

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 A0A077LQB4
Elsewhere: RCSB PDB 4ZGC · PDBe 4ZGC · UniProt A0A077LQB4

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