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Structure of leishmania nucleoside diphostate kinase mutant P95S

Analyse Structure of leishmania nucleoside diphostate kinase mutant P95S in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5C7P
Type: protein
Length: 434 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nucleoside diphosphate kinase
EC: 2.7.4.6
UniProt: Q9U1E1
Pockets: 7 · best druggability 0.58

Structure

x-ray diffraction · 3 distinct chains · 46% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nucleoside diphosphate kinase (EC 2.7.4.6)	protein	144	48% helix, 17% strand	Q9U1E1
B	Nucleoside diphosphate kinase (EC 2.7.4.6)	protein	146	45% helix, 18% strand	Q9U1E1
C	Nucleoside diphosphate kinase (EC 2.7.4.6)	protein	144	46% helix, 18% strand	Q9U1E1

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	226	0.58	0.80	35	empty
2	82	0.48	0.82	25	empty
3	149	0.42	0.74	27	empty
4	132	0.41	0.75	21	empty
5	110	0.39	0.75	23	empty

Interfaces

2 interfaces between chains.

A–B · 986 Å² buried · 18 hydrogen bonds · protein-protein
B–C · 762 Å² buried · 6 hydrogen bonds · protein-protein

Compared structures

5C7P · Structure of Leishmania nucleoside diphostate kinase mutant P95S · 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 Q9U1E1
Elsewhere: RCSB PDB 5C7P · PDBe 5C7P · UniProt Q9U1E1

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