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Structure of T-cell surface glycoprotein CD4, trigonal crystal form

Analyse Structure of T-cell surface glycoprotein CD4, trigonal crystal form in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1WIQ
Type: protein
Length: 726 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: T-cell surface glycoprotein CD4
UniProt: P01730
Pockets: 8 · best druggability 0.61

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	T-cell surface glycoprotein CD4	protein	363	5% helix, 50% strand	P01730

Pockets

8 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	115	0.61	0.86	25	empty
2	153	0.60	0.84	28	empty
3	113	0.59	0.85	21	empty
4	112	0.58	0.85	21	empty
5	142	0.40	0.74	24	empty

Interfaces

1 interface between chains.

A–B · 576 Å² buried · 13 hydrogen bonds · protein-protein

Compared structures

1WIQ · Structure of T-cell surface glycoprotein CD4, trigonal crystal form · the same entry in another collection · chain A against A, TM-score 1.00
P01730 · AlphaFold monomer V2.0 prediction for T-cell surface glycoprotein CD4 (P01730) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 P01730
Elsewhere: RCSB PDB 1WIQ · PDBe 1WIQ · UniProt P01730

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