GL1X · GenesisL1 explorer

MolNFT v1 · #5882 · protein

Human factor xiii with calcium bound in the ion site

1EVU · Coagulation factor xiii: “Human factor xiii with calcium bound in the ion site”. X-ray diffraction, 1 ligand (CA), 17 pockets (best druggability 0.86). MolNFT v1 #5882 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
1EVU
Type
protein
Length
1,416 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
Ligands
CA
Pockets
17 · best druggability 0.86

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
ACoagulation factor xiii (EC 2.3.2.13)protein70815% helix, 41% strandP00488
BCoagulation factor xiii (EC 2.3.2.13)protein70815% helix, 42% strandP00488

Ligands and binding sites

  • CA · Calcium ion · metal · 2 copies · chains A, B
  • PGO · S-1,2-propanediol · additive · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19770.860.87124PGO
28220.850.88104empty
34530.680.8039empty
41300.650.8828empty
51280.610.8635empty

Interfaces

1 interface between chains.

  • A–B · 2894 Ų buried · 48 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 modified (acetylation).

Compared structures

  • 1EVU · Human factor xiii with calcium bound in the ion site · 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 B against A, TM-score 0.99

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