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Solution NMR structure of cyclin-dependent kinase 2-associated protein 2 (CDK2AP2, doc-1R) from homo sapiens, northeast structural genomics consortium (nesg) target HR8910C

Analyse Solution NMR structure of cyclin-dependent kinase 2-associated protein 2… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2M1L
Type: protein
Length: 138 residues
Chains: 2
Method: solution nmr
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cyclin-dependent kinase 2-associated protein 2
UniProt: O75956
Pockets: 1 · best druggability 0.28

Structure

solution nmr · 1 distinct chain · 64% helix, 0% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Cyclin-dependent kinase 2-associated protein 2	protein	69	64% helix, 0% strand	O75956

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	52	0.28	0.75	12	empty

Interfaces

1 interface between chains.

A–B · 2072 Å² buried · 29 hydrogen bonds · protein-protein

Compared structures

2M1L · Solution NMR Structure of Cyclin-dependent kinase 2-associated protein 2 (CDK2AP2… · the same entry in another collection · chain A against A, TM-score 1.00
O75956 · AlphaFold monomer V2.0 prediction for cyclin-dependent kinase 2-associated protein 2… · a predicted model of the same protein · chain A against A, TM-score 0.70

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 O75956
Elsewhere: RCSB PDB 2M1L · PDBe 2M1L · UniProt O75956

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