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The crystal structure of the haemophilus influenzae hxua secretion domain involved in the two-partner secretion pathway

Analyse The crystal structure of the haemophilus influenzae hxua secretion domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4I84
Type: protein
Length: 570 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: HEME/HEMOPEXIN-binding protein
UniProt: P44602
Pockets: 2 · best druggability 0.74

Structure

x-ray diffraction · 2 distinct chains · 1% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	HEME/HEMOPEXIN-binding protein	protein	296	1% helix, 56% strand	P44602
B	HEME/HEMOPEXIN-binding protein	protein	274	0% helix, 59% strand	P44602

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	57	0.74	0.99	23	empty
2	96	0.46	0.80	24	empty

Interfaces

1 interface between chains.

A–B · 854 Å² buried · 26 hydrogen bonds · protein-protein

Compared structures

4I84 · The crystal structure of the Haemophilus influenzae HxuA secretion domain involved in the… · the same entry in another collection · chain A against A, TM-score 1.00
P44602 · AlphaFold monomer V2.0 prediction for HEME/HEMOPEXIN-binding protein (P44602) · a predicted model of the same protein · chain B 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 P44602
Elsewhere: RCSB PDB 4I84 · PDBe 4I84 · UniProt P44602

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