10RK
Heparin-induced trans tetrameric complex of VEGF, VEGFR2 and Neuropilin 1
This is a non-PDB format compatible entry.
Functional Information from PROSITE/UniProt
| site_id | PS00249 |
| Number of Residues | 13 |
| Details | PDGF_1 Platelet-derived growth factor (PDGF) family signature. PSCVplmRCAGCC |
| Chain | Residue | Details |
| A | PRO74-CYS86 |
| site_id | PS00740 |
| Number of Residues | 41 |
| Details | MAM_1 MAM domain signature. GnFIysqAdenqkgkvar.LvspvVysqssahCMtFwYhmsG |
| Chain | Residue | Details |
| E | GLY690-GLY730 |
| site_id | PS01285 |
| Number of Residues | 30 |
| Details | FA58C_1 Coagulation factors 5/8 type C domain (FA58C) signature 1. GWtpgedsyke......WIqVDlgllrfVtaVgTQG |
| Chain | Residue | Details |
| E | GLY314-GLY343 | |
| E | GLY470-GLY502 |
| site_id | PS01286 |
| Number of Residues | 17 |
| Details | FA58C_2 Coagulation factors 5/8 type C domain (FA58C) signature 2. Pvswetgis..MRfEVyGC |
| Chain | Residue | Details |
| E | PRO408-CYS424 | |
| E | PRO566-CYS583 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 456 |
| Details | Domain: {"description":"CUB 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00059","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 472 |
| Details | Domain: {"description":"CUB 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00059","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 596 |
| Details | Domain: {"description":"F5/8 type C 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 304 |
| Details | Domain: {"description":"F5/8 type C 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00081","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O14786","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 64 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 8 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19656770","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 264 |
| Details | Domain: {"description":"Ig-like C2-type 2"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 396 |
| Details | Domain: {"description":"Ig-like C2-type 3"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 344 |
| Details | Domain: {"description":"Ig-like C2-type 4"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 476 |
| Details | Domain: {"description":"Ig-like C2-type 5"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 344 |
| Details | Domain: {"description":"Ig-like C2-type 7"} |
| Chain | Residue | Details |
