Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

7KVE

Cryo-EM structure of human Factor V at 3.3 Angstrom resolution

Functional Information from GO Data
ChainGOidnamespacecontents
B0005507molecular_functioncopper ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005788cellular_componentendoplasmic reticulum lumen
B0005886cellular_componentplasma membrane
B0007596biological_processblood coagulation
B0008015biological_processblood circulation
B0016020cellular_componentmembrane
B0030134cellular_componentCOPII-coated ER to Golgi transport vesicle
B0031091cellular_componentplatelet alpha granule
B0031093cellular_componentplatelet alpha granule lumen
B0032571biological_processresponse to vitamin K
B0033116cellular_componentendoplasmic reticulum-Golgi intermediate compartment membrane
B0046872molecular_functionmetal ion binding
B1903561cellular_componentextracellular vesicle
Functional Information from PROSITE/UniProt
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GkWiIsSlTPkhLqAGMqayI
ChainResidueDetails
BGLY276-ILE296
BGLY1852-PHE1872

site_idPS01285
Number of Residues34
DetailsFA58C_1 Coagulation factors 5/8 type C domain (FA58C) signature 1. AWsveklaaefaskp..WIqVDmqkeviItgIqTQG
ChainResidueDetails
BALA1919-GLY1952
BALA2083-GLY2112

site_idPS01286
Number of Residues17
DetailsFA58C_2 Coagulation factors 5/8 type C domain (FA58C) signature 2. Ptraynrpt..LRlELqGC
ChainResidueDetails
BPRO2017-CYS2033
BPRO2177-CYS2193

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
BASP111
BASP112
BHIS1815
BHIS1817

site_idSWS_FT_FI2
Number of Residues4
DetailsSITE: Cleavage; by activated protein C => ECO:0000269|PubMed:7989361
ChainResidueDetails
BARG306
BARG506
BARG679
BLYS994

site_idSWS_FT_FI3
Number of Residues3
DetailsSITE: Cleavage; by thrombin => ECO:0000269|PubMed:3110773
ChainResidueDetails
BARG709
BARG1018
BARG1545

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19690332
ChainResidueDetails
BTHR612

site_idSWS_FT_FI5
Number of Residues7
DetailsMOD_RES: Sulfotyrosine => ECO:0000255
ChainResidueDetails
BTYR665
BTYR696
BTYR698
BTYR1494
BTYR1510
BTYR1515
BTYR1565

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
BSER831

site_idSWS_FT_FI7
Number of Residues21
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN23
BASN748
BASN754
BASN910
BASN1046
BASN1055
BASN1075
BASN1078
BASN1451
BASN1471
BASN1675
BASN27
BASN1982
BASN2181
BASN211
BASN354
BASN440
BASN526
BASN713
BASN724
BASN732

site_idSWS_FT_FI8
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:16335952
ChainResidueDetails
BASN269

site_idSWS_FT_FI9
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:16335952
ChainResidueDetails
BASN432
BASN793
BASN949
BASN1531

222926

PDB entries from 2024-07-24

PDB statisticsPDBj update infoContact PDBjnumon