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The structure of hcinap-mgadp-pi complex at 2.0 ångströms resolution

Analyse The structure of hcinap-mgadp-pi complex at 2.0 ångströms resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3IIL
Type: protein
Length: 175 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Coilin-interacting nuclear ATPase protein
EC: 2.7.4.3
UniProt: Q5F2S9
Ligands: ADP, MG, LI, SO4, PO4
Pockets: 1 · best druggability 0.59

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Coilin-interacting nuclear ATPase protein (EC 2.7.4.3)	protein	175	52% helix, 18% strand	Q5F2S9

Ligands and binding sites

ADP · Adenosine-5'-diphosphate · ligand · chains A
MG · Magnesium ion · metal · 3 copies · chains A
LI · Lithium ion · metal · chains A
SO4 · Sulfate ion · ion · 4 copies · chains A
PO4 · Phosphate ion · ion · chains A

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

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	447	0.59	0.75	42	LI, ADP, MG, PO4

Compared structures

3IIL · The structure of hCINAP-MgADP-Pi complex at 2.0 angstroms resolution · the same entry in another collection · chain A against A, TM-score 1.00

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 Q5F2S9
Elsewhere: RCSB PDB 3IIL · PDBe 3IIL · UniProt Q5F2S9

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