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MPLUM-E16P

Analyse MPLUM-E16P in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4H3L
Type: protein
Length: 425 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Fluorescent protein plum
UniProt: Q5S3G7
Ligands: NRQ, NA
Pockets: 5 · best druggability 0.75

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 58% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Fluorescent protein plum	protein	213	5% helix, 58% strand	Q5S3G7
B	Fluorescent protein plum	protein	212	5% 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
NA · Sodium ion · metal · chains A

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

Pockets

5 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	81	0.75	0.98	26	NRQ
2	73	0.73	0.97	25	NRQ
3	191	0.51	0.77	33	empty
4	60	0.50	0.86	24	empty
5	189	0.50	0.77	32	empty

Interfaces

1 interface between chains.

A–B · 775 Å² buried · 12 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 cofactor (chromophore).

Compared structures

4H3L · mPlum-E16P · 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 4H3L · PDBe 4H3L · UniProt Q5S3G7

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