MolNFT v1 · #153341 · protein

Cryo-EM structure and transport mechanism of a wall teichoic acid ABC transporter

6JBH · Tarh: “Cryo-EM structure and transport mechanism of a wall teichoic acid ABC transporter”. Electron microscopy, 17 pockets (best druggability 0.83). MolNFT v1 #153341 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 6JBH
Type: protein
Length: 1,062 residues
Chains: 4
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Tarh; Targ
Pockets: 17 · best druggability 0.83

Structure

electron microscopy · 2 distinct chains · 47% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Tarh	protein	264	38% helix, 16% strand	—
C, D	Targ	protein	267	57% helix, 0% strand	—

Pockets

17 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1125	0.83	0.84	115	empty
2	1051	0.82	0.84	107	empty
3	963	0.82	0.83	77	empty
4	735	0.74	0.79	76	empty
5	195	0.60	0.82	31	empty

Interfaces

6 interfaces between chains.

A–B · 1436 Å² buried · 18 hydrogen bonds · protein-protein
C–D · 1133 Å² buried · 7 hydrogen bonds · protein-protein
A–D · 1034 Å² buried · 8 hydrogen bonds · protein-protein
B–C · 1030 Å² buried · 7 hydrogen bonds · protein-protein
A–C · 265 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

6JBH · Cryo-EM structure and transport mechanism of a wall teichoic acid ABC transporter · 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
Elsewhere: RCSB PDB 6JBH · PDBe 6JBH

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