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The crystal structure of modified bovine fibrinogen (at ~4 ångström resolution)

Analyse The crystal structure of modified bovine fibrinogen (at ~4 ångström resolution) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1DEQ
Type
protein
Length
3,900 residues
Chains
14
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Fibrinogen (alpha chain); Fibrinogen (beta chain); Fibrinogen (gamma chain); Fibrinogen
UniProt
P02672, P02676, P12799
Pockets
13 · best druggability 0.34

Structure

x-ray diffraction · 4 distinct chains · 0% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, D, N, QFibrinogen (alpha chain)protein1800% helix, 0% strandP02672
B, E, O, RFibrinogen (beta chain)protein3800% helix, 0% strandP02676
C, F, P, SFibrinogen (gamma chain)protein3700% helix, 0% strandP12799
M, ZFibrinogenprotein900% helix, 0% strand—

Pockets

13 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1770.340.7319empty
2780.340.7323empty
3660.330.7426empty
4730.330.7326empty
5700.320.7321empty

Interfaces

25 interfaces between chains.

  • O–P · 294 Ų buried · 0 hydrogen bonds · protein-protein
  • B–C · 267 Ų buried · 0 hydrogen bonds · protein-protein
  • E–F · 242 Ų buried · 0 hydrogen bonds · protein-protein
  • Q–R · 232 Ų buried · 0 hydrogen bonds · protein-protein
  • A–B · 217 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 1DEQ · The crystal structure of modified bovine fibrinogen (at ~4 ångström resolution) · the same entry in another collection · chain F against F, TM-score 1.00

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