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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9I2H

A 3.3 angstrom cryo-EM structure of an engineered high-affinity human prothrombinase complex

This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CkDglgeYtCtC
ChainResidueDetails
LCYS61-CYS72
site_idPS00011
Number of Residues26
DetailsGLA_1 Vitamin K-dependent carboxylation domain. EcmEEtCsyeearEvfedsdktne.FW
ChainResidueDetails
LGLU16-TRP41
site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CtCleGfeGKnC
ChainResidueDetails
LCYS70-CYS81
site_idPS00079
Number of Residues21
DetailsMULTICOPPER_OXIDASE1 Multicopper oxidases signature 1. GkWiIsSlTPkhLqAGMqayI
ChainResidueDetails
AGLY276-ILE296
BGLY1852-PHE1872
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. LTAAHC
ChainResidueDetails
HLEU53-CYS58
site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DAcqGDSGGPHV
ChainResidueDetails
HASP189-VAL200
site_idPS01186
Number of Residues12
DetailsEGF_2 EGF-like domain signature 2. CtCleGFegkn....C
ChainResidueDetails
LCYS70-CYS81
LCYS109-CYS124
site_idPS01187
Number of Residues25
DetailsEGF_CA Calcium-binding EGF-like domain signature. DgDQCetsp..........Cqnqgk..CkDglgeYtC
ChainResidueDetails
LASP46-CYS70
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 Residues232
DetailsDomain: {"description":"Peptidase S1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00274","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues3
DetailsActive site: {"description":"Charge relay system"}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues44
DetailsDomain: {"description":"Gla","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues36
DetailsDomain: {"description":"EGF-like 1; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues40
DetailsDomain: {"description":"EGF-like 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues11
DetailsModified residue: {"description":"4-carboxyglutamate","evidences":[{"source":"PROSITE-ProRule","id":"PRU00463","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"(3R)-3-hydroxyaspartate","evidences":[{"source":"PubMed","id":"6871167","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues299
DetailsDomain: {"description":"F5/8 type A 1"}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues163
DetailsDomain: {"description":"Plastocyanin-like 1"}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues126
DetailsDomain: {"description":"Plastocyanin-like 2"}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues336
DetailsDomain: {"description":"F5/8 type A 2"}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues178
DetailsDomain: {"description":"Plastocyanin-like 3"}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues148
DetailsDomain: {"description":"Plastocyanin-like 4"}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues2
DetailsSite: {"description":"Cleavage; by activated protein C","evidences":[{"source":"PubMed","id":"7989361","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues2
DetailsModified residue: {"description":"Sulfotyrosine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues9
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16335952","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues329
DetailsDomain: {"description":"F5/8 type A 3"}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues173
DetailsDomain: {"description":"Plastocyanin-like 5"}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues146
DetailsDomain: {"description":"Plastocyanin-like 6"}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues154
DetailsDomain: {"description":"F5/8 type C 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues155
DetailsDomain: {"description":"F5/8 type C 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247947

PDB entries from 2026-01-21

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