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Crystal structural of native escu C-terminal domain

Analyse Crystal structural of native escu C-terminal domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3BZL
Type: protein
Length: 219 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Escu
UniProt: Q9AJ26
Ligands: NA
Pockets: 1 · best druggability 0.65

Structure

x-ray diffraction · 4 distinct chains · 47% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Escu	protein	18	44% helix, 22% strand	Q9AJ26
C	Escu	protein	81	49% helix, 21% strand	Q9AJ26
B	Escu	protein	38	39% helix, 11% strand	Q9AJ26
D	Escu	protein	82	49% helix, 21% strand	Q9AJ26

Ligands and binding sites

NA · Sodium ion · metal · chains C
FMT · Formic acid · additive · chains B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	291	0.65	0.81	33	empty

Interfaces

3 interfaces between chains.

B–D · 1125 Å² buried · 20 hydrogen bonds · protein-protein
A–C · 1116 Å² buried · 19 hydrogen bonds · protein-protein
C–D · 564 Å² buried · 4 hydrogen bonds · protein-protein

Compared structures

3BZL · Crystal structural of native EscU C-terminal domain · 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 Q9AJ26
Elsewhere: RCSB PDB 3BZL · PDBe 3BZL · UniProt Q9AJ26

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