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Structure of P. falciparum PFPK5

Analyse Structure of P. falciparum PFPK5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1OB3
Type: protein
Length: 535 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division control protein 2 homolog
EC: 2.7.1.-
UniProt: Q07785
Pockets: 9 · best druggability 0.70

Structure

x-ray diffraction · 2 distinct chains · 39% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cell division control protein 2 homolog (EC 2.7.1.-)	protein	277	38% helix, 17% strand	Q07785
B	Cell division control protein 2 homolog (EC 2.7.1.-)	protein	258	40% helix, 15% strand	Q07785

Pockets

9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	196	0.70	0.88	25	empty
2	220	0.70	0.86	28	empty
3	341	0.59	0.77	31	empty
4	160	0.47	0.76	32	empty
5	109	0.39	0.75	21	empty

Interfaces

1 interface between chains.

A–B · 99 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1OB3 · Structure of P. falciparum PfPK5 · the same entry in another collection · chain A against A, TM-score 1.00
Q07785 · AlphaFold monomer V2.0 prediction for cell division control protein 2 homolog (Q07785) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q07785
Elsewhere: RCSB PDB 1OB3 · PDBe 1OB3 · UniProt Q07785

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