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Crystal structure of the drbd and crops of tcda

Analyse Crystal structure of the drbd and crops of tcda in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7U1Z
Type: protein
Length: 3,232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Toxin a
EC: 3.4.22.-
UniProt: P16154
Ligands: SO4
Pockets: 20 · best druggability 0.82

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 41% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Toxin a (EC 3.4.22.-)	protein	1612	15% helix, 41% strand	P16154
A	Toxin a (EC 3.4.22.-)	protein	1620	15% helix, 41% strand	P16154

Ligands and binding sites

SO4 · Sulfate ion · ion · 36 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, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1014	0.82	0.83	102	empty
2	1047	0.82	0.83	110	empty
3	901	0.73	0.78	82	empty
4	861	0.73	0.78	91	empty
5	56	0.69	0.97	20	empty

Interfaces

1 interface between chains.

B–A · 3708 Å² buried · 27 hydrogen bonds · protein-protein

Compared structures

7U1Z · Crystal structure of the DRBD and CROPs of TcdA · 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 P16154
Elsewhere: RCSB PDB 7U1Z · PDBe 7U1Z · UniProt P16154

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