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Crystal structure of helicobacter pylori ATP dependent protease, ftsh

Analyse Crystal structure of helicobacter pylori ATP dependent protease, ftsh in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2R62
Type: protein
Length: 498 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division protease ftsh homolog
EC: 3.4.24.-
UniProt: P71408
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cell division protease ftsh homolog (EC 3.4.24.-)	protein	249	28% helix, 4% strand	P71408

Pockets

4 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	128	0.65	0.87	27	empty
2	160	0.63	0.85	28	empty
3	64	0.37	0.79	19	empty
4	83	0.35	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 392 Å² buried · 16 hydrogen bonds · protein-protein

Compared structures

2R62 · Crystal structure of Helicobacter pylori ATP dependent protease, FtsH · the same entry in another collection · chain B against B, TM-score 1.00
P71408 · AlphaFold monomer V2.0 prediction for ATP-dependent zinc metalloprotease ftsh (P71408) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P71408
Elsewhere: RCSB PDB 2R62 · PDBe 2R62 · UniProt P71408

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