MolNFT v1 · #93477 · protein

Mplumayc-E16A

4H3M · Fluorescent protein plum: “Mplumayc-E16A”. X-ray diffraction, 1 ligand (NRQ), 7 pockets (best druggability 0.77). MolNFT v1 #93477 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 4H3M
Type: protein
Length: 423 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fluorescent protein plum
UniProt: Q5S3G7
Ligands: NRQ
Pockets: 7 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 3% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fluorescent protein plum	protein	212	3% helix, 58% strand	Q5S3G7
B	Fluorescent protein plum	protein	211	3% helix, 58% strand	Q5S3G7

Ligands and binding sites

NRQ · {(4Z)-4-(4-hydroxybenzylidene)-2-[3-(methylthio) propanimidoyl]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid · ligand · 2 copies · chains A, B

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

Pockets

7 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	94	0.77	0.97	28	NRQ
2	93	0.76	0.97	26	NRQ
3	168	0.54	0.80	30	empty
4	85	0.41	0.79	18	empty
5	87	0.38	0.77	19	empty

Interfaces

1 interface between chains.

A–B · 648 Å² buried · 8 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor (chromophore).

Compared structures

4H3M · mPlumAYC-E16A · 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 Q5S3G7
Elsewhere: RCSB PDB 4H3M · PDBe 4H3M · UniProt Q5S3G7

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.