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Crystal structure of extracellular part of human epcam

Analyse Crystal structure of extracellular part of human epcam in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4MZV
Type: protein
Length: 243 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epithelial cell adhesion molecule
UniProt: P16422
Pockets: 3 · best druggability 0.69

Structure

x-ray diffraction · 1 distinct chain · 17% helix, 27% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epithelial cell adhesion molecule	protein	243	17% helix, 27% strand	P16422

Ligands and binding sites

DMU · Decyl-beta-D-maltopyranoside · 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, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	183	0.69	0.87	25	DMU
2	282	0.58	0.78	42	empty
3	170	0.55	0.80	33	empty

Modifications

Observed in the structure: 6 disulfide, 1 modified (disulfide, cyclization).

Compared structures

4MZV · Crystal structure of extracellular part of human EpCAM · the same entry in another collection · chain A against A, TM-score 1.00
P16422 · AlphaFold monomer V2.0 prediction for epithelial cell adhesion molecule (P16422) · a predicted model of the same protein · chain A against A, TM-score 0.94

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 P16422
Elsewhere: RCSB PDB 4MZV · PDBe 4MZV · UniProt P16422

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