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Crystal structure of human crmp-2 without C-terminal tail

Analyse Crystal structure of human crmp-2 without C-terminal tail in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5X1C
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: Q16555
Pockets: 8 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 36% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dihydropyrimidinase-related protein 2	protein	484	36% helix, 23% strand	Q16555
B	Dihydropyrimidinase-related protein 2	protein	477	36% helix, 24% strand	Q16555

Pockets

8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	878	0.85	0.87	98	empty
2	186	0.64	0.85	34	empty
3	170	0.61	0.84	26	empty
4	177	0.60	0.82	23	empty
5	232	0.48	0.74	24	empty

Interfaces

1 interface between chains.

A–B · 1280 Å² buried · 22 hydrogen bonds · protein-protein

Compared structures

5X1C · Crystal Structure of Human CRMP-2 without C-terminal Tail · the same entry in another collection · chain A against A, TM-score 1.00
Q16555 · AlphaFold monomer V2.0 prediction for dihydropyrimidinase-related protein 2 (Q16555) · 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 Q16555
Elsewhere: RCSB PDB 5X1C · PDBe 5X1C · UniProt Q16555

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