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9OZH

Cryo-EM structure of 1:2:1 ROS1/NEL/NICOL holo-complex, conformation 2.

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. CvNtpgsFmCiC
ChainResidueDetails
BCYS457-CYS468
BCYS572-CYS583
BCYS619-CYS630

site_idPS00022
Number of Residues12
DetailsEGF_1 EGF-like domain signature 1. CaCpqGftGPsC
ChainResidueDetails
BCYS541-CYS552

site_idPS00107
Number of Residues30
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGEVYeGtaldiladgsgesr....VAVK
ChainResidueDetails
DLEU1967-LYS1996

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV
ChainResidueDetails
DPHE2091-VAL2103

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYkndYYR
ChainResidueDetails
DASP2125-ARG2133

site_idPS01186
Number of Residues15
DetailsEGF_2 EGF-like domain signature 2. CiCktGYiriddys.C
ChainResidueDetails
BCYS466-CYS480
BCYS508-CYS521
BCYS541-CYS552
BCYS663-CYS677

site_idPS01187
Number of Residues27
DetailsEGF_CA Calcium-binding EGF-like domain signature. DvDECaegqhy........Crentm..CvNtpgsFmC
ChainResidueDetails
BASP440-CYS466
BASP555-CYS581
BASP602-CYS628

site_idPS01208
Number of Residues40
DetailsVWFC_1 VWFC domain signature. Ckn.CTCmngtvq........CealiCslsd......Cppnsalsyvdgk....CCke..C
ChainResidueDetails
BCYS291-CYS330
BCYS719-CYS755

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues326
DetailsDomain: {"description":"Laminin G-like"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues118
DetailsDomain: {"description":"VWFC 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00220","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues84
DetailsDomain: {"description":"EGF-like 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues82
DetailsDomain: {"description":"EGF-like 2; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues80
DetailsDomain: {"description":"EGF-like 3; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues60
DetailsDomain: {"description":"EGF-like 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues92
DetailsDomain: {"description":"EGF-like 5; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues110
DetailsDomain: {"description":"VWFC 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00220","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues116
DetailsDomain: {"description":"VWFC 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00220","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues13
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues35
DetailsDomain: {"description":"EGF-like 6; calcium-binding","evidences":[{"source":"PROSITE-ProRule","id":"PRU00076","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

249697

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