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Bacterial asc transporter crystal structure in open to in conformation

Analyse Bacterial asc transporter crystal structure in open to in conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6F2G
Type: protein
Length: 561 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative amino ACID/POLYAMINE transport protein; Nanobody 74
UniProt: A8UCQ5
Ligands: ZN
Pockets: 2 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 60% helix, 11% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative amino ACID/POLYAMINE transport protein	protein	430	76% helix, 0% strand	A8UCQ5
B	Nanobody 74	protein	131	9% helix, 47% strand	—

Ligands and binding sites

ZN · Zinc ion · metal · chains B

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

Pockets

2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	785	0.77	0.81	83	empty
2	164	0.54	0.80	24	empty

Interfaces

1 interface between chains.

A–B · 1203 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

6F2G · Bacterial asc transporter crystal structure in open to in conformation · 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 A8UCQ5
Elsewhere: RCSB PDB 6F2G · PDBe 6F2G · UniProt A8UCQ5

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