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Crystal structure of mouse CRMP2

Analyse Crystal structure of mouse CRMP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5UQC
Type: protein
Length: 961 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Dihydropyrimidinase-related protein 2
UniProt: O08553
Ligands: 1PG
Pockets: 10 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydropyrimidinase-related protein 2	protein	482	36% helix, 23% strand	O08553
B	Dihydropyrimidinase-related protein 2	protein	479	37% helix, 23% strand	O08553

Ligands and binding sites

1PG · 2-(2-{2-[2-(2-methoxy-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanol · ligand · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	677	0.85	0.90	74	empty
2	250	0.64	0.82	30	empty
3	245	0.63	0.81	36	empty
4	175	0.60	0.82	23	empty
5	148	0.59	0.84	20	empty

Interfaces

1 interface between chains.

A–B · 1253 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

5UQC · Crystal structure of mouse CRMP2 · the same entry in another collection · chain A against A, TM-score 1.00
O08553 · AlphaFold monomer V2.0 prediction for dihydropyrimidinase-related protein 2 (O08553) · a predicted model of the same protein · chain B against A, TM-score 1.00

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Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt O08553
Elsewhere: RCSB PDB 5UQC · PDBe 5UQC · UniProt O08553

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