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The heme-bound structure of the chloroplast protein AT3G03890

Analyse The heme-bound structure of the chloroplast protein AT3G03890 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6M0A
Type
protein
Length
1,016 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
AT3G03890 protein
UniProt
Q8LDU1
Ligands
HEM, AZI
Pockets
12 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 36% helix, 33% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAT3G03890 proteinprotein25536% helix, 33% strandQ8LDU1
B, CAT3G03890 proteinprotein25636% helix, 33% strandQ8LDU1
DAT3G03890 proteinprotein24935% helix, 32% strandQ8LDU1

Ligands and binding sites

  • HEM · Protoporphyrin IX containing Fe · ligand · 4 copies · chains A, B, C, D
  • AZI · Azide ion · ion · 4 copies · chains A, B, C, D

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111980.800.82120HEM
29160.770.7994empty
34380.730.8347HEM, AZI
44170.720.8348HEM
54010.710.8243HEM

Interfaces

3 interfaces between chains.

  • C–D · 1507 Ų buried · 18 hydrogen bonds · protein-protein
  • A–B · 1484 Ų buried · 17 hydrogen bonds · protein-protein
  • B–D · 221 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 6M0A · The heme-bound structure of the chloroplast protein At3g03890 · the same entry in another collection · chain A against A, TM-score 1.00

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