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Crystal structure of pii from synechocystis sp. pcc 6803

Analyse Crystal structure of pii from synechocystis sp. pcc 6803 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1UL3
Type
protein
Length
378 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Nitrogen regulatory protein P-II
UniProt
Q55247
Ligands
CA
Pockets
6 · best druggability 0.59

Structure

x-ray diffraction · 3 distinct chains · 29% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANitrogen regulatory protein P-IIprotein9528% helix, 39% strandQ55247
B, CNitrogen regulatory protein P-IIprotein9429% helix, 40% strandQ55247
DNitrogen regulatory protein P-IIprotein9529% helix, 38% strandQ55247

Ligands and binding sites

  • CA · Calcium ion · metal · 2 copies · chains B, C
  • GOL · Glycerol · additive · 2 copies · chains A, C

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12430.590.8031empty
22500.580.7933GOL
31520.500.7832empty
4900.430.7924empty
5500.320.7711empty

Interfaces

3 interfaces between chains.

  • A–C · 1106 Ų buried · 16 hydrogen bonds · protein-protein
  • B–C · 1072 Ų buried · 17 hydrogen bonds · protein-protein
  • A–B · 1042 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 1UL3 · Crystal Structure of PII from Synechocystis sp. PCC 6803 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q55247 · AlphaFold monomer V2.0 prediction for nitrogen regulatory protein P-II (Q55247) · a predicted model of the same protein · chain B against A, TM-score 0.93

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