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Structure of the extra-membranous domain of the secretin hofq from actinobacillus actinomycetemcomitans

Analyse Structure of the extra-membranous domain of the secretin hofq from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2Y3M
Type: protein
Length: 273 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein transport protein hofq
UniProt: C9R226
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 32% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein transport protein hofq	protein	135	31% helix, 34% strand	C9R226
B	Protein transport protein hofq	protein	138	33% helix, 36% strand	C9R226

Ligands and binding sites

GOL · Glycerol · additive · 2 copies · chains A, B
FMT · Formic acid · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	65	0.28	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 2016 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

2Y3M · Structure of the extra-membranous domain of the secretin HofQ from Actinobacillus… · 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 C9R226
Elsewhere: RCSB PDB 2Y3M · PDBe 2Y3M · UniProt C9R226

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