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Crystal structures of the burkholderia multivorans hopanoid transporter hpnn

Analyse Crystal structures of the burkholderia multivorans hopanoid transporter hpnn in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5KHS
Type: protein
Length: 1,705 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative rnd superfamily efflux pump membrane protein
UniProt: A0A0H3KP92
Pockets: 20 · best druggability 0.86

Structure

x-ray diffraction · 2 distinct chains · 68% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Putative rnd superfamily efflux pump membrane protein	protein	853	67% helix, 4% strand	A0A0H3KP92
A	Putative rnd superfamily efflux pump membrane protein	protein	852	68% helix, 4% strand	A0A0H3KP92

Pockets

20 pockets found on a 1 Å grid, 10 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1064	0.86	0.87	93	empty
2	1100	0.86	0.87	90	empty
3	1074	0.81	0.81	88	empty
4	1075	0.80	0.81	95	empty
5	73	0.75	0.98	21	empty

Interfaces

1 interface between chains.

B–A · 2067 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

5KHS · Crystal structures of the Burkholderia multivorans hopanoid transporter HpnN · the same entry in another collection · chain B against B, 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 A0A0H3KP92
Elsewhere: RCSB PDB 5KHS · PDBe 5KHS · UniProt A0A0H3KP92

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