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Crystal structure of human ed-4F2HC

Analyse Crystal structure of human ed-4F2HC in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2DH2
Type: protein
Length: 421 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: 4F2 cell-surface antigen heavy chain
UniProt: P08195
Pockets: 3 · best druggability 0.60

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 19% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	4F2 cell-surface antigen heavy chain	protein	421	35% helix, 19% strand	P08195

Ligands and binding sites

ACT · Acetate ion · 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	268	0.60	0.79	38	empty
2	148	0.43	0.75	21	empty
3	50	0.26	0.74	19	empty

Modifications

Observed in the structure: 4 modified (engineered).

Compared structures

2DH2 · Crystal Structure of human ED-4F2hc · the same entry in another collection · chain A against A, TM-score 1.00
P08195 · AlphaFold monomer V2.0 prediction for 4F2 cell-surface antigen heavy chain (P08195) · a predicted model of the same protein · chain A 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 P08195
Elsewhere: RCSB PDB 2DH2 · PDBe 2DH2 · UniProt P08195

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