Research workbench

Cryo-EM structure of human factor V at 3.3 ångström resolution

Analyse Cryo-EM structure of human factor V at 3.3 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7KVE
Type: protein
Length: 1,374 residues
Chains: 1
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Coagulation factor V
UniProt: P12259
Pockets: 20 · best druggability 0.84

Structure

electron microscopy · 1 distinct chain · 5% helix, 28% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
B	Coagulation factor V	protein	1374	5% helix, 28% strand	P12259

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	993	0.84	0.85	87	empty
2	899	0.75	0.79	79	empty
3	811	0.74	0.79	84	empty
4	885	0.73	0.77	79	empty
5	255	0.71	0.86	31	empty

Modifications

Observed in the structure: 6 disulfide (disulfide).

Compared structures

7KVE · Cryo-EM structure of human Factor V at 3.3 Angstrom resolution · the same entry in another collection · chain B against B, TM-score 1.00
P12259 · AlphaFold monomer V2.0 prediction for coagulation factor V (P12259) · a predicted model of the same protein · chain B against A, TM-score 0.92

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P12259
Elsewhere: RCSB PDB 7KVE · PDBe 7KVE · UniProt P12259

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