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

7PFP

Full-length cryo-EM structure of the native human uromodulin (UMOD)/Tamm-Horsfall protein (THP) filament

Functional Information from GO Data
ChainGOidnamespacecontents
A0005509molecular_functioncalcium ion binding
B0005509molecular_functioncalcium ion binding
C0005509molecular_functioncalcium ion binding
Functional Information from PROSITE/UniProt
site_idPS00010
Number of Residues12
DetailsASX_HYDROXYL Aspartic acid and asparagine hydroxylation site. CvNtpgsFsCvC
ChainResidueDetails
ACYS83-CYS94
ACYS126-CYS137

site_idPS00682
Number of Residues41
DetailsZP_1 ZP domain signature. VgtmldggDlsrFaLlMtnCYaTPss..NaTdplkyfIIqdr.C
ChainResidueDetails
AVAL487-CYS527

site_idPS01186
Number of Residues14
DetailsEGF_2 EGF-like domain signature 2. CtCqeGFtgdglt..C
ChainResidueDetails
ACYS50-CYS63
ACYS92-CYS106
ACYS135-CYS150

site_idPS01187
Number of Residues28
DetailsEGF_CA Calcium-binding EGF-like domain signature. DlDECaipgahn.......Csanss..CvNtpgsFsC
ChainResidueDetails
AASP65-CYS92
AASP108-CYS135

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsSITE: Cleavage => ECO:0000269|PubMed:18375198
ChainResidueDetails
APHE587
BPHE587
CPHE587

site_idSWS_FT_FI2
Number of Residues3
DetailsLIPID: GPI-anchor amidated serine => ECO:0000255
ChainResidueDetails
ASER614
BSER614
CSER614

site_idSWS_FT_FI3
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:32616672
ChainResidueDetails
AASN38
BASN38
CASN38

site_idSWS_FT_FI4
Number of Residues6
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:32616672, ECO:0000269|PubMed:35273390, ECO:0007744|PDB:7PFP, ECO:0007744|PDB:7Q3N
ChainResidueDetails
BASN80
CASN76
CASN80
AASN76
AASN80
BASN76

site_idSWS_FT_FI5
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:26811476, ECO:0000269|PubMed:32616672, ECO:0000269|PubMed:35273390, ECO:0007744|PDB:7PFP, ECO:0007744|PDB:7Q3N
ChainResidueDetails
AASN232
BASN232
CASN232

site_idSWS_FT_FI6
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine => ECO:0000269|PubMed:32616672, ECO:0000269|PubMed:35273390, ECO:0007744|PDB:7PFP, ECO:0007744|PDB:7Q3N
ChainResidueDetails
AASN275
BASN275
CASN275

site_idSWS_FT_FI7
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:32616672, ECO:0000269|PubMed:33196145, ECO:0000269|PubMed:35273390, ECO:0007744|PDB:6TQK, ECO:0007744|PDB:6TQL, ECO:0007744|PDB:7PFP
ChainResidueDetails
AASN322
BASN322
CASN322

site_idSWS_FT_FI8
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (complex) asparagine => ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:32616672, ECO:0000269|PubMed:32815518, ECO:0000269|PubMed:33196145, ECO:0000269|PubMed:35273390, ECO:0007744|PDB:6TQK, ECO:0007744|PDB:6TQL, ECO:0007744|PDB:6ZS5, ECO:0007744|PDB:6ZYA, ECO:0007744|PDB:7PFP
ChainResidueDetails
AASN396
BASN396
CASN396

site_idSWS_FT_FI9
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) (high mannose) asparagine; alternate => ECO:0000269|PubMed:32616672, ECO:0000269|PubMed:32815518, ECO:0000269|PubMed:33196145, ECO:0007744|PDB:6TQK, ECO:0007744|PDB:6TQL, ECO:0007744|PDB:6ZS5, ECO:0007744|PDB:6ZYA, ECO:0007744|PDB:7PFP
ChainResidueDetails
AASN513
BASN513
CASN513

219869

PDB entries from 2024-05-15

PDB statisticsPDBj update infoContact PDBjnumon