MolNFT v1 · #115435 · protein

The structural basis for CDC42-induced dimerization of iqgaps

5CJP · Cell division cycle 42 (GTP binding protein, 25KDA)…: “The structural basis for CDC42-induced dimerization of iqgaps”. X-ray diffraction, 2 ligands (GTP, MG), 14 pockets (best druggability 0.87). MolNFT v1 #115435 on GenesisL1: 3D…

PDB: 5CJP
Type: protein
Length: 1,452 residues
Chains: 6
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cell division cycle 42 (GTP binding protein, 25KDA), isoform CRA_A; RAS…
UniProt: A0A024RAE4, Q13576
Ligands: GTP, MG
Pockets: 14 · best druggability 0.87

Structure

x-ray diffraction · 2 distinct chains · 58% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C, D	Cell division cycle 42 (GTP binding protein, 25KDA), isoform CRA_A	protein	177	40% helix, 24% strand	A0A024RAE4
E, F	RAS GTPase-activating-like protein IQGAP2	protein	372	67% helix, 2% strand	Q13576

Ligands and binding sites

GTP · Guanosine-5'-triphosphate · ligand · 4 copies · chains A, E, B, F, C, D
MG · Magnesium ion · metal · 4 copies · chains A, B, C, D

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

Pockets

14 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1012	0.87	0.88	123	GTP, MG
2	851	0.86	0.88	99	empty
3	1020	0.86	0.87	125	GTP, MG
4	263	0.80	0.92	46	empty
5	367	0.80	0.89	58	GTP, MG

Interfaces

10 interfaces between chains.

E–F · 2054 Å² buried · 24 hydrogen bonds · protein-protein
A–E · 1676 Å² buried · 22 hydrogen bonds · protein-protein
C–E · 1575 Å² buried · 19 hydrogen bonds · protein-protein
D–F · 1563 Å² buried · 15 hydrogen bonds · protein-protein
B–F · 1532 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

Q13576 · AlphaFold monomer V2.0 prediction for RAS GTPase-activating-like protein IQGAP2 (Q13576) · a predicted model of the same protein · chain E against A, TM-score 0.80

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 A0A024RAE4
Every structure of UniProt Q13576
Elsewhere: RCSB PDB 5CJP · PDBe 5CJP · UniProt A0A024RAE4 · UniProt Q13576

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