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Crystal structure of the hopq-CEACAM1 complex

Analyse Crystal structure of the hopq-CEACAM1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6AW2
Type: protein
Length: 460 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Carcinoembryonic antigen-related cell adhesion molecule 1; Hopq
UniProt: P13688, H6A3H4
Pockets: 1 · best druggability 0.56

Structure

x-ray diffraction · 2 distinct chains · 40% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Carcinoembryonic antigen-related cell adhesion molecule 1	protein	107	6% helix, 52% strand	P13688
B	Hopq	protein	353	50% helix, 13% strand	H6A3H4

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	182	0.56	0.80	29	empty

Interfaces

1 interface between chains.

A–B · 1015 Å² buried · 14 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 disulfide (disulfide).

Compared structures

6AW2 · Crystal structure of the HopQ-CEACAM1 complex · the same entry in another collection · chain A against A, TM-score 1.00
P13688 · AlphaFold monomer V2.0 prediction for carcinoembryonic antigen- related cell adhesion… · a predicted model of the same protein · chain A against A, TM-score 0.98

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 P13688
Every structure of UniProt H6A3H4
Elsewhere: RCSB PDB 6AW2 · PDBe 6AW2 · UniProt P13688 · UniProt H6A3H4

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