MolNFT v1 · #93938 · protein

Crystal structure of engineered protein. northeast structural genomics consortium target OR280.

4HHU: “Crystal structure of engineered protein. northeast structural genomics consortium target OR280.”. X-ray diffraction, 1 ligand (AE4), 3 pockets (best druggability 0.58). MolNFT v1 #93938 on GenesisL1: 3D structure, binding sites and…

PDB: 4HHU
Type: protein
Length: 336 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: OR280
Ligands: AE4
Pockets: 3 · best druggability 0.58

Structure

x-ray diffraction · 2 distinct chains · 42% helix, 35% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	OR280	protein	170	41% helix, 36% strand	—
B	OR280	protein	166	42% helix, 34% strand	—

Ligands and binding sites

AE4 · 3,6,9,12,15-pentaoxaheptadecan-1-ol · ligand · chains A, B
PG4 · Tetraethylene glycol · additive · 2 copies · chains B, A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	221	0.58	0.80	34	empty
2	311	0.56	0.76	24	PG4
3	64	0.42	0.81	14	AE4

Interfaces

1 interface between chains.

A–B · 1013 Å² buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 14 modified (engineered).

Compared structures

4HHU · Crystal Structure of Engineered Protein. Northeast Structural Genomics Consortium Target… · 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
Elsewhere: RCSB PDB 4HHU · PDBe 4HHU

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