MolNFT v1 · #63477 · protein

Crystal structure of the gap-related domain of IQGAP1

3FAY · RAS GTPase-activating-like protein IQGAP1: “Crystal structure of the gap-related domain of IQGAP1”. X-ray diffraction, 3 pockets (best druggability 0.50). MolNFT v1 #63477 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 3FAY
Type: protein
Length: 379 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: RAS GTPase-activating-like protein IQGAP1
UniProt: P46940
Pockets: 3 · best druggability 0.50

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	RAS GTPase-activating-like protein IQGAP1	protein	379	67% helix, 0% strand	P46940

Ligands and binding sites

TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	56	0.50	0.87	19	empty
2	84	0.41	0.78	14	empty
3	68	0.32	0.75	18	empty

Modifications

Observed in the structure: 10 modified (engineered).

Compared structures

3FAY · Crystal structure of the GAP-related domain of IQGAP1 · the same entry in another collection · chain A against A, TM-score 1.00
P46940 · AlphaFold monomer V2.0 prediction for RAS GTPase-activating-like protein IQGAP1 (P46940) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P46940
Elsewhere: RCSB PDB 3FAY · PDBe 3FAY · UniProt P46940

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