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Crystal structure at 2.8 ångströms resolution of a soluble form of the cell adhesion molecule CD2

Analyse Crystal structure at 2.8 ångströms resolution of a soluble form of the cell… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1HNG
Type: protein
Length: 350 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: CD2
UniProt: P08921
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 54% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	CD2	protein	175	2% helix, 54% strand	P08921

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	62	0.34	0.77	14	empty

Interfaces

1 interface between chains.

A–B · 614 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide (disulfide).

Compared structures

1HNG · Crystal structure at 2.8 ångströms resolution of a soluble form of the cell adhesion… · the same entry in another collection · chain A against A, TM-score 1.00
P08921 · AlphaFold monomer V2.0 prediction for T-cell surface antigen CD2 (P08921) · a predicted model of the same protein · chain B against A, TM-score 0.99

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 P08921
Elsewhere: RCSB PDB 1HNG · PDBe 1HNG · UniProt P08921

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