MolNFT v1 · #124122 · protein

Crystal structure of truncated flgd (monoclinic form) from the human pathogen helicobacter pylori (strain 26695)

5K5Y · Basal-body rod modification protein flgd: “Crystal structure of truncated flgd (monoclinic form) from the human pathogen helicobacter pylori (strain…”. X-ray diffraction, 4 pockets (best druggability 0.65). MolNFT v1 #124122 on…

PDB: 5K5Y
Type: protein
Length: 584 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Basal-body rod modification protein flgd
UniProt: O25565
Pockets: 4 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 49% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Basal-body rod modification protein flgd	protein	146	4% helix, 49% strand	O25565

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	679	0.65	0.74	57	empty
2	518	0.60	0.74	42	empty
3	52	0.26	0.74	13	empty
4	53	0.24	0.72	11	empty

Interfaces

3 interfaces between chains.

A–B · 498 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 219 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 92 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

5K5Y · Crystal structure of truncated FlgD (monoclinic form) from the human pathogen… · 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 O25565
Elsewhere: RCSB PDB 5K5Y · PDBe 5K5Y · UniProt O25565

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