MolNFT v1 · #19119 · protein

Structure of a heterophilic adhesion complex between the human CD2 and CD58(LFA-3) counter-receptors

1QA9 · Human CD2 protein: “Structure of a heterophilic adhesion complex between the human CD2 and CD58(LFA-3) counter-receptors”. X-ray diffraction, 4 pockets (best druggability 0.68). MolNFT v1 #19119 on GenesisL1: 3D structure, binding…

PDB: 1QA9
Type: protein
Length: 394 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Human CD2 protein; Human CD58 protein
Pockets: 4 · best druggability 0.68

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 47% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C	Human CD2 protein	protein	102	0% helix, 50% strand	—
B, D	Human CD58 protein	protein	95	3% helix, 44% strand	—

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	339	0.68	0.82	44	empty
2	181	0.67	0.86	26	empty
3	64	0.44	0.82	13	empty
4	74	0.33	0.75	17	empty

Interfaces

3 interfaces between chains.

A–B · 752 Å² buried · 20 hydrogen bonds · protein-protein
C–D · 744 Å² buried · 18 hydrogen bonds · protein-protein
A–C · 32 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

1QA9 · Structure of a Heterophilic Adhesion Complex Between the Human CD2 and CD58(LFA-3)… · 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
Elsewhere: RCSB PDB 1QA9 · PDBe 1QA9

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