MolNFT v1 · #163456 · protein

Kima from bacillus subtilis in inward-facing, occluded state

6S3K · Apc family permease: “Kima from bacillus subtilis in inward-facing, occluded state”. Electron microscopy, 1 ligand (K), 20 pockets (best druggability 0.74). MolNFT v1 #163456 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 6S3K
Type: protein
Length: 1,146 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Apc family permease
UniProt: A0A164U4X9
Ligands: K
Pockets: 20 · best druggability 0.74

Structure

electron microscopy · 1 distinct chain · 60% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B, A	Apc family permease	protein	573	60% helix, 4% strand	A0A164U4X9

Ligands and binding sites

K · Potassium ion · metal · 6 copies · chains B, A

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

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	834	0.74	0.78	53	empty
2	787	0.73	0.78	50	empty
3	329	0.64	0.80	43	K
4	399	0.64	0.78	43	empty
5	308	0.62	0.78	31	empty

Interfaces

1 interface between chains.

B–A · 3051 Å² buried · 10 hydrogen bonds · protein-protein

Compared structures

6S3K · KimA from Bacillus subtilis in inward-facing, occluded state · 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 A0A164U4X9
Elsewhere: RCSB PDB 6S3K · PDBe 6S3K · UniProt A0A164U4X9

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