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Heme exporter hrtba in complex with heme

Analyse Heme exporter hrtba in complex with heme in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7W7D
Type: protein
Length: 3,369 residues
Chains: 12
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative ABC transport system, ATP-binding protein; Putative ABC transport system…
UniProt: Q6NEF2, Q6NEF1
Ligands: HEM
Pockets: 20 · best druggability 0.81

Structure

x-ray diffraction · 9 distinct chains · 43% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative ABC transport system, ATP-binding protein	protein	216	36% helix, 26% strand	Q6NEF2
B, H	Putative ABC transport system integral membrane protein	protein	341	54% helix, 19% strand	Q6NEF1
C	Putative ABC transport system, ATP-binding protein	protein	218	35% helix, 28% strand	Q6NEF2
D, J, L	Putative ABC transport system integral membrane protein	protein	343	53% helix, 19% strand	Q6NEF1
E	Putative ABC transport system, ATP-binding protein	protein	217	35% helix, 23% strand	Q6NEF2
F	Putative ABC transport system integral membrane protein	protein	342	53% helix, 19% strand	Q6NEF1
G	Putative ABC transport system, ATP-binding protein	protein	225	33% helix, 26% strand	Q6NEF2
I	Putative ABC transport system, ATP-binding protein	protein	221	33% helix, 28% strand	Q6NEF2
K	Putative ABC transport system, ATP-binding protein	protein	219	35% helix, 28% strand	Q6NEF2

Ligands and binding sites

HEM · Protoporphyrin IX containing Fe · ligand · 2 copies · chains B, D, F, H

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

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1009	0.81	0.83	106	HEM
2	972	0.80	0.82	76	empty
3	1177	0.79	0.81	111	HEM
4	975	0.79	0.81	101	empty
5	868	0.78	0.81	86	empty

Interfaces

17 interfaces between chains.

B–D · 2109 Å² buried · 10 hydrogen bonds · protein-protein
F–H · 2096 Å² buried · 16 hydrogen bonds · protein-protein
J–L · 1225 Å² buried · 4 hydrogen bonds · protein-protein
E–F · 1179 Å² buried · 8 hydrogen bonds · protein-protein
A–B · 1116 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

7W7D · Heme exporter HrtBA in complex with heme · 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 Q6NEF2
Every structure of UniProt Q6NEF1
Elsewhere: RCSB PDB 7W7D · PDBe 7W7D · UniProt Q6NEF2 · UniProt Q6NEF1

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