MolNFT v1 · #90400 · protein

Crystal structure of bacillus cereus tubz, GDP-form

4EI7 · Plasmid replication protein repx: “Crystal structure of bacillus cereus tubz, GDP-form”. X-ray diffraction, 1 ligand (GDP), 5 pockets (best druggability 0.81). MolNFT v1 #90400 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 4EI7
Type: protein
Length: 763 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Plasmid replication protein repx
UniProt: Q74P24
Ligands: GDP
Pockets: 5 · best druggability 0.81

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 20% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Plasmid replication protein repx	protein	382	49% helix, 20% strand	Q74P24
B	Plasmid replication protein repx	protein	381	48% helix, 20% strand	Q74P24

Ligands and binding sites

GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	994	0.81	0.82	80	GDP
2	481	0.62	0.76	61	GDP
3	232	0.57	0.79	42	empty
4	216	0.55	0.78	41	empty
5	112	0.39	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 1110 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

4EI7 · Crystal structure of Bacillus cereus TubZ, GDP-form · the same entry in another collection · chain A against A, TM-score 1.00
Q74P24 · AlphaFold monomer V2.0 prediction for tubulin-like protein tubz (Q74P24) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 Q74P24
Elsewhere: RCSB PDB 4EI7 · PDBe 4EI7 · UniProt Q74P24

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