MolNFT v1 · #89021 · protein

Crystal structure of B. subtilis enga in complex with GDP

4DCU · GTP-binding protein enga: “Crystal structure of B. subtilis enga in complex with GDP”. X-ray diffraction, 1 ligand (GDP), 6 pockets (best druggability 0.73). MolNFT v1 #89021 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 4DCU
Type: protein
Length: 400 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: GTP-binding protein enga
UniProt: P50743
Ligands: GDP
Pockets: 6 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 37% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	GTP-binding protein enga	protein	400	37% helix, 24% strand	P50743

Ligands and binding sites

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

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

Pockets

6 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	786	0.73	0.79	56	empty
2	256	0.73	0.87	40	empty
3	120	0.36	0.73	18	empty
4	52	0.33	0.78	13	empty
5	50	0.31	0.77	13	empty

Compared structures

4DCU · Crystal Structure of B. subtilis EngA in complex with GDP · the same entry in another collection · chain A against A, TM-score 1.00
P50743 · AlphaFold monomer V2.0 prediction for GTPase der (P50743) · a predicted model of the same protein · chain A against A, TM-score 0.65

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 P50743
Elsewhere: RCSB PDB 4DCU · PDBe 4DCU · UniProt P50743

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