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Three-dimensional structure of a transglutaminase: human blood coagulation factor xiii

Analyse Three-dimensional structure of a transglutaminase: human blood coagulation… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1GGT
Type
protein
Length
1,418 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Coagulation factor xiii
EC
2.3.2.13
UniProt
P00488
Pockets
20 · best druggability 0.67

Structure

x-ray diffraction · 2 distinct chains · 15% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ACoagulation factor xiii (EC 2.3.2.13)protein71015% helix, 41% strandP00488
BCoagulation factor xiii (EC 2.3.2.13)protein70814% helix, 41% strandP00488

Pockets

20 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16400.670.7667empty
21090.620.8724empty
3970.600.8723empty
41150.600.8625empty
52090.530.7738empty

Interfaces

1 interface between chains.

  • A–B · 958 Ų buried · 2 hydrogen bonds · protein-protein

Compared structures

  • 1GGT · Three-dimensional structure of a transglutaminase: human blood coagulation factor xiii · the same entry in another collection · chain A against A, TM-score 1.00
  • P00488 · AlphaFold monomer V2.0 prediction for coagulation factor xiii a chain (P00488) · a predicted model of the same protein · chain A against A, TM-score 0.99

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