MolNFT v1 · #24009 · protein

Crystal structure of N-aequorin

1UHK · Aequorin 2: “Crystal structure of N-aequorin”. X-ray diffraction, 1 ligand (CZN), 4 pockets (best druggability 0.84). MolNFT v1 #24009 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 1UHK
Type: protein
Length: 382 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Aequorin 2
UniProt: P02592
Ligands: CZN
Pockets: 4 · best druggability 0.84

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Aequorin 2	protein	191	61% helix, 5% strand	P02592

Ligands and binding sites

CZN · (2S,8R)-8-benzyl-2-hydroperoxy-6-(4-hydroxyphenyl)-2-(2-naphthylmethyl)-7,8-dihydroimidazo[1,2-a]pyrazin-3(2H)-one · ligand · 2 copies · chains A, B

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

Pockets

4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	200	0.84	0.97	31	CZN
2	195	0.83	0.96	29	CZN
3	242	0.51	0.75	29	empty
4	65	0.29	0.73	14	empty

Interfaces

1 interface between chains.

A–B · 171 Å² buried · 1 hydrogen bond · protein-protein

Compared structures

1UHK · Crystal structure of n-aequorin · the same entry in another collection · chain A against A, TM-score 1.00
P02592 · AlphaFold monomer V2.0 prediction for aequorin-2 (P02592) · a predicted model of the same protein · chain A against A, TM-score 0.96

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 P02592
Elsewhere: RCSB PDB 1UHK · PDBe 1UHK · UniProt P02592

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