MolNFT v1 · #7751 · protein

Crystal structure of the protein 4.1R membrane binding domain

1GG3 · Erythroid membrane protein 4.1R: “Crystal structure of the protein 4.1R membrane binding domain”. X-ray diffraction, 11 pockets (best druggability 0.79). MolNFT v1 #7751 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1GG3
Type: protein
Length: 837 residues
Chains: 3
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Erythroid membrane protein 4.1R
UniProt: P11171
Pockets: 11 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B, C	Erythroid membrane protein 4.1R	protein	279	36% helix, 19% strand	P11171

Pockets

11 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	949	0.79	0.81	108	empty
2	704	0.73	0.79	71	empty
3	202	0.61	0.82	34	empty
4	211	0.51	0.77	40	empty
5	162	0.49	0.78	19	empty

Interfaces

2 interfaces between chains.

A–C · 827 Å² buried · 14 hydrogen bonds · protein-protein
A–B · 806 Å² buried · 11 hydrogen bonds · protein-protein

Compared structures

1GG3 · Crystal structure of the protein 4.1R membrane binding domain · the same entry in another collection · chain A against A, TM-score 1.00
P11171 · AlphaFold monomer V2.0 prediction for protein 4.1 (P11171) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P11171
Elsewhere: RCSB PDB 1GG3 · PDBe 1GG3 · UniProt P11171

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