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Integral membrane domain of autotransporter hbp

Analyse Integral membrane domain of autotransporter hbp in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3AEH
Type: protein
Length: 554 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Hemoglobin-binding protease hbp autotransporter
EC: 3.4.21.-
UniProt: O88093
Pockets: 9 · best druggability 0.76

Structure

x-ray diffraction · 1 distinct chain · 11% helix, 69% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Hemoglobin-binding protease hbp autotransporter (EC 3.4.21.-)	protein	277	11% helix, 69% strand	O88093

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	205	0.76	0.91	44	empty
2	305	0.76	0.88	47	empty
3	220	0.52	0.78	40	empty
4	204	0.52	0.77	32	empty
5	130	0.44	0.77	22	empty

Interfaces

1 interface between chains.

A–B · 1266 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

3AEH · Integral membrane domain of autotransporter Hbp · the same entry in another collection · chain A against A, TM-score 1.00
O88093 · AlphaFold monomer V2.0 prediction for hemoglobin-binding protease hbp autotransporter… · a predicted model of the same protein · chain A against A, TM-score 0.94

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 O88093
Elsewhere: RCSB PDB 3AEH · PDBe 3AEH · UniProt O88093

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