3U7D: KRIT1/CCM1 FERM domain

Crystal structure of the KRIT1/CCM1 FERM domain in complex with the heart of glass (HEG1) cytoplasmic tail. Determined by X-ray diffraction at 2.49 Å resolution. Released 12 Sept 2012.

Method
X-ray diffraction
Resolution
2.49 Å
Organism
Homo sapiens
Chains
4
Atoms
5,136
Mol. weight
81.09 kDa
Released
12 Sept 2012

Explore 3U7D in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3U7D contains 31 α-helices and 24 β-strands across 2 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: 15 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand421-42551
β-strand431-43551
α-helix439-4413
α-helix444-4507
α-helix457-4593
β-strand461-46771
β-strand470-47341
α-helix474-4752
α-helix480-4856
α-helix487-4948
β-strand505-51061
α-helix516-5194
α-helix525-54117
α-helix548-56316
α-helix581-5833
α-helix594-5974
α-helix598-61013
α-helix618-62912
α-helix6371
β-strand638-64582
β-strand655-66392
β-strand666-67162
β-strand677-68262
β-strand686-69052
β-strand696-70162
β-strand707-71152
α-helix715-72713
Chain C: 16 helices, 12 β-strands
ElementResiduesLengthSheet
β-strand421-42553
β-strand431-43553
α-helix439-4413
α-helix444-4507
β-strand461-46773
β-strand470-47343
α-helix474-4752
α-helix480-4856
α-helix487-4948
α-helix499-5013
β-strand505-51063
α-helix516-5194
α-helix525-54016
α-helix548-56316
α-helix568-5714
α-helix578-5814
α-helix594-5974
α-helix598-60912
α-helix618-62912
α-helix6371
β-strand638-64474
β-strand656-66274
β-strand666-67164
β-strand677-68264
β-strand686-69054
β-strand696-70164
β-strand707-71154
α-helix715-72612

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Krev interaction trapped protein 1A, Cprotein322Homo sapiensO00522 (AlphaFold model)
Protein HEG homolog 1B, Dprotein26Homo sapiensQ9ULI3 (AlphaFold model)
Sequence of entity 1 (A, C), FASTA
>3U7D_1 Krev interaction trapped protein 1 (chains A, C)
GAKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQL
KPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDE
ARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKA
PHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHK
VIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQ
AGLVVKLLMKLNGQLMPTERNS
Sequence of entity 2 (B, D), FASTA
>3U7D_2 Protein HEG homolog 1 (chains B, D)
SRHSCIFPGQYNPSFISDESRRRDYF

Primary citation

Structural basis of the junctional anchorage of the cerebral cavernous malformations complex. Gingras, A.R., Liu, J.J., Ginsberg, M.H. J Cell Biol (2012) 199:39-48. DOI 10.1083/jcb.201205109 · PubMed

Other PDB entries of the same protein (UniProt O00522 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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