1KF9: PDB entry 1KF9

Phage display derived variant of human growth hormone complexed with two copies of the extracellular domain of its receptor. Determined by X-ray diffraction at 2.6 Å resolution. Released 20 Nov 2002.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
6
Atoms
8,678
Mol. weight
153.61 kDa
Released
20 Nov 2002

Explore 1KF9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1KF9 contains 33 α-helices and 70 β-strands across 6 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 9 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix6-3530
α-helix38-403
α-helix43-464
α-helix64-696
α-helix74-8512
α-helix89-935
α-helix94-985
α-helix109-12719
α-helix157-18125
Chain B: 4 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand235-23951
β-strand24012
β-strand246-25051
β-strand265-27063
β-strand281-28223
β-strand293-29641
β-strand306-31273
β-strand317-32483
α-helix325-3284
β-strand32912
α-helix331-3344
β-strand335-344104
β-strand350-35894
β-strand372-38095
α-helix3861
β-strand387-38825
α-helix389-3913
β-strand39215
β-strand396-40384
β-strand407-416105
β-strand41915
β-strand429-43245
Chain C: 3 helices, 17 β-strands
ElementResiduesLengthSheet
β-strand535-53956
β-strand54017
β-strand546-55056
β-strand567-57048
β-strand581-58228
β-strand593-59646
β-strand607-61048
β-strand622-62328
β-strand62917
α-helix631-6344
β-strand635-644109
β-strand650-65899
β-strand672-680910
β-strand687-688210
α-helix689-6902
β-strand692110
β-strand696-70389
β-strand707-7161010
α-helix727-7282
β-strand729-732410
Chain D: 9 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix1006-103530
α-helix1038-10403
α-helix1043-10453
α-helix1064-10696
α-helix1074-108512
α-helix1089-10935
α-helix1094-10985
α-helix1109-112719
α-helix1157-118125
Chain E: 4 helices, 18 β-strands
ElementResiduesLengthSheet
β-strand1235-1239511
β-strand1240112
β-strand1246-1250511
β-strand1265-1270613
β-strand1281-1282213
β-strand1293-1296411
β-strand1306-1312713
β-strand1317-1324813
α-helix1325-13284
β-strand1329112
α-helix1331-13344
β-strand1335-13441014
β-strand1350-1358914
β-strand1372-1380915
α-helix13861
β-strand1387-1388215
α-helix1389-13913
β-strand1392115
β-strand1396-1403814
β-strand1407-14161015
β-strand1419115
β-strand1429-1432415
Chain F: 4 helices, 17 β-strands
ElementResiduesLengthSheet
β-strand1535-1539516
β-strand1540117
β-strand1546-1550516
β-strand1565-1570618
β-strand1581-1582218
β-strand1593-1596416
β-strand1607-1612618
β-strand1617-1623718
β-strand1629117
α-helix1631-16344
β-strand1635-16441019
β-strand1650-1658919
β-strand1672-1680920
α-helix16861
β-strand1687-1688220
α-helix1689-16902
β-strand1692120
β-strand1696-1703819
β-strand1707-17161020
α-helix1727-17282
β-strand1729-1732420

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Phage display derived variant human growth hormoneA, Dprotein191Homo sapiensP01241 (AlphaFold model)
Extracellular domain human growth hormone receptor (1-238)B, C, E, Fprotein238Homo sapiensP10912 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>1KF9_1 PHAGE DISPLAY DERIVED VARIANT HUMAN GROWTH HORMONE (chains A, D)
FPTIPLSRLADNAWLRADRLNQLAFDTYQEFEEAYIPKEQIHSFWWNPQTSLCPSESIPT
PSNKEETQQKSNLELLRISLLLIQSWLEPVQFLRSVFANSLVYGASDSNVYDLLKDLEEG
IQTLMGRLEDGSPRTGQIFKQTYSKFDTNSHNDDALLKNYGLLYCFNKDMSKVSTYLRTV
QCRSVEGSCGF
Sequence of entity 2 (B, C, E, F), FASTA
>1KF9_2 EXTRACELLULAR DOMAIN HUMAN GROWTH HORMONE RECEPTOR (1-238) (chains B, C, E, F)
FSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKN
LGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDE
KCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKE
VNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQ

Primary citation

Structure of a Phage Display Derived Variant of Human Growth Hormone Complexed to Two Copies of the Extracellular Domain of its Receptor: Evidence for Strong Structural Coupling between Receptor Binding Sites. Schiffer, C.A., Ultsch, M., Walsh, S. et al. J Mol Biol (2002) 316:277-289. DOI 10.1006/jmbi.2001.5348 · PubMed

Other PDB entries of the same protein (UniProt P01241 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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