Research workbench

GTPase domain of septin 10 from schistosoma mansoni in complex with GTP

Analyse GTPase domain of septin 10 from schistosoma mansoni in complex with GTP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4KVA
Type: protein
Length: 504 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Septin
UniProt: G4VFI8
Ligands: GTP, MG
Pockets: 4 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 41% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Septin	protein	246	41% helix, 20% strand	G4VFI8
B	Septin	protein	258	41% helix, 22% strand	G4VFI8

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 2 copies · chains A, B
MG · Magnesium ion · metal · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	410	0.71	0.82	51	empty
2	227	0.56	0.79	39	GTP
3	214	0.56	0.79	44	GTP
4	73	0.30	0.73	15	empty

Interfaces

1 interface between chains.

A–B · 972 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

4KVA · GTPase domain of Septin 10 from Schistosoma mansoni in complex with GTP · 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 G4VFI8
Elsewhere: RCSB PDB 4KVA · PDBe 4KVA · UniProt G4VFI8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.