MolNFT v1 · #87133 · protein

Legionella pneumophila NTPDASE1 crystal form IV (part-open)

4BRO · Ectonucleoside triphosphate diphosphohydrolase I: “Legionella pneumophila NTPDASE1 crystal form IV (part-open)”. X-ray diffraction, 7 pockets (best druggability 0.78). MolNFT v1 #87133 on GenesisL1: 3D structure, binding sites and…

PDB: 4BRO
Type: protein
Length: 702 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Ectonucleoside triphosphate diphosphohydrolase I
EC: 3.6.1.5
UniProt: Q5ZUA2
Pockets: 7 · best druggability 0.78

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 25% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Ectonucleoside triphosphate diphosphohydrolase I (EC 3.6.1.5)	protein	351	40% helix, 25% strand	Q5ZUA2
B	Ectonucleoside triphosphate diphosphohydrolase I (EC 3.6.1.5)	protein	351	39% helix, 26% strand	Q5ZUA2

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	881	0.78	0.81	80	empty
2	263	0.66	0.83	47	empty
3	201	0.58	0.81	28	empty
4	225	0.58	0.80	27	empty
5	133	0.51	0.80	26	empty

Interfaces

1 interface between chains.

A–B · 1583 Å² buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

4BRO · Legionella pneumophila NTPDase1 crystal form IV (part-open) · 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 Q5ZUA2
Elsewhere: RCSB PDB 4BRO · PDBe 4BRO · UniProt Q5ZUA2

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