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X-ray structure of branchiostoma floridae fluorescent protein LANFP10A

Analyse X-ray structure of branchiostoma floridae fluorescent protein LANFP10A in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6M9X
Type
protein
Length
860 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fluorescent protein LANFP10A
UniProt
C3YRA2
Ligands
JBY
Pockets
11 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 56% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DFluorescent protein LANFP10Aprotein21510% helix, 56% strandC3YRA2

Ligands and binding sites

  • JBY · (2S)-2-{(4Z)-2-(aminomethyl)-4-[(4-hydroxyphenyl) methylidene]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}propanoic acid · ligand · 4 copies · chains A, B, C, D

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

Pockets

11 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19720.870.89101empty
2970.770.9731JBY
3960.760.9727JBY
4840.750.9829JBY
5710.730.9720JBY

Interfaces

6 interfaces between chains.

  • C–D · 1216 Ų buried · 9 hydrogen bonds · protein-protein
  • A–B · 1204 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 1003 Ų buried · 18 hydrogen bonds · protein-protein
  • A–C · 998 Ų buried · 20 hydrogen bonds · protein-protein
  • A–D · 92 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 8 covalent (covalent ligand).

Compared structures

  • 6M9X · X-ray Structure of Branchiostoma floridae fluorescent protein lanFP10A · the same entry in another collection · chain A against A, TM-score 1.00

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