MolNFT v1 · #121183 · protein

The structure of the kdo-capped saccharide binding subunit of the O-12 specific ABC transporter, wzt

5HNP: “The structure of the kdo-capped saccharide binding subunit of the O-12 specific ABC transporter, wzt”. X-ray diffraction, 1 ligand (CL), 3 pockets (best druggability 0.31). MolNFT v1 #121183 on GenesisL1: 3D structure, binding sites…

PDB: 5HNP
Type: protein
Length: 327 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: ABC transporter
UniProt: A0A0B5INH8
Ligands: CL
Pockets: 3 · best druggability 0.31

Structure

x-ray diffraction · 2 distinct chains · 8% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	ABC transporter	protein	161	9% helix, 55% strand	A0A0B5INH8
B	ABC transporter	protein	166	8% helix, 52% strand	A0A0B5INH8

Ligands and binding sites

CL · Chloride ion · ion · chains A

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	63	0.31	0.75	19	empty
2	75	0.30	0.74	21	empty
3	70	0.29	0.73	21	empty

Interfaces

1 interface between chains.

A–B · 1404 Å² buried · 32 hydrogen bonds · protein-protein

Compared structures

5HNP · The structure of the kdo-capped saccharide binding subunit of the O-12 specific ABC… · 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 A0A0B5INH8
Elsewhere: RCSB PDB 5HNP · PDBe 5HNP · UniProt A0A0B5INH8

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