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Crystal structure of the stage V sporulation protein ad (spovad) from bacillus licheniformis. northeast structural genomics consortium target BIR6.

Analyse Crystal structure of the stage V sporulation protein ad (spovad) from bacillus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3LMA
Type
protein
Length
1,258 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Stage V sporulation protein ad (spovad)
UniProt
Q65HU8
Pockets
14 · best druggability 0.78

Structure

x-ray diffraction · 4 distinct chains · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AStage V sporulation protein ad (spovad)protein30938% helix, 25% strandQ65HU8
BStage V sporulation protein ad (spovad)protein31139% helix, 24% strandQ65HU8
CStage V sporulation protein ad (spovad)protein32737% helix, 23% strandQ65HU8
DStage V sporulation protein ad (spovad)protein31140% helix, 24% strandQ65HU8

Pockets

14 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19340.780.81106empty
2770.610.9019empty
31550.520.7931empty
41380.500.7921empty
5670.490.8422empty

Interfaces

5 interfaces between chains.

  • B–C · 2426 Ų buried · 27 hydrogen bonds · protein-protein
  • A–D · 2270 Ų buried · 35 hydrogen bonds · protein-protein
  • A–C · 482 Ų buried · 10 hydrogen bonds · protein-protein
  • B–D · 135 Ų buried · 0 hydrogen bonds · protein-protein
  • C–D · 102 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 32 modified (engineered).

Compared structures

  • 3LMA · Crystal structure of the stage V sporulation protein AD (SpoVAD) from Bacillus… · the same entry in another collection · chain A against A, TM-score 1.00

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