6UZK: Ternary Complex of KRIT1

Crystal Structure of the Ternary Complex of KRIT1 bound to both the Rap1 GTPase and HKi6. Determined by X-ray diffraction at 1.92 Å resolution. Released 18 Nov 2020.

Method: X-ray diffraction
Resolution: 1.92 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,942
Mol. weight: 57.14 kDa
Ligands: GNP, MG, QMA
Released: 18 Nov 2020

Explore 6UZK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6UZK contains 20 α-helices and 20 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: 14 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	420-425	6	1
β-strand	431-436	6	1
α-helix	439-441	3
α-helix	444-449	6
α-helix	455-458	4
β-strand	461-467	7	1
β-strand	470-473	4	1
α-helix	480-485	6
α-helix	487-494	8
β-strand	505-510	6	1
α-helix	516-520	5
α-helix	525-541	17
α-helix	548-563	16
α-helix	568-571	4
α-helix	578-581	4
α-helix	594-597	4
α-helix	598-610	13
α-helix	618-629	12
β-strand	638-645	8	2
β-strand	655-662	8	2
β-strand	666-671	6	2
β-strand	677-682	6	2
β-strand	687-690	4	2
β-strand	696-701	6	2
β-strand	706-711	6	2
α-helix	715-727	13

Chain B: 6 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	2-9	8	1
α-helix	16-25	10
β-strand	37-46	10	1
β-strand	49-58	10	1
α-helix	68-74	7
β-strand	77-83	7	1
α-helix	87-91	5
α-helix	93-104	12
β-strand	111-116	6	1
α-helix	128-137	10
β-strand	142-145	4	1
β-strand	147	1	3
β-strand	152	1	3
α-helix	154-165	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Krev interaction trapped protein 1	A	protein	322	Homo sapiens	O00522 (AlphaFold model)
Ras-related protein Rap-1b	B	protein	167	Homo sapiens	P61224 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>6UZK_1 Krev interaction trapped protein 1 (chains A)
GAKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQL
KPYHKPLQHVRDWPEILAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDE
ARYNLLKGFYTAPDAKLITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKA
PHWTNRILHEYKNLSTSEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHK
VIPVYVGVNIKGLHLLNMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQ
AGLVVKLLMKLNGQLMPTERNS

Sequence of entity 2 (B), FASTA

>6UZK_2 Ras-related protein Rap-1b (chains B)
MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDAQQCMLEILDTAG
TEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTDDVPMILVGNKCDL
EDERVVGKEQGQNLARQWNNCAFLESSAKSKINVNEIFYDLVRQINR

Ligands and cofactors

ID	Name	Formula	Copies
GNP	Phosphoaminophosphonic acid-guanylate ester	C10 H17 N6 O13 P3	1
MG	Magnesium ion	Mg	1
QMA	2-hydroxy-6-methoxynaphthalene-1-carbaldehyde	C12 H10 O3	1

Primary citation

Inhibition of the HEG1-KRIT1 interaction increases KLF4 and KLF2 expression in endothelial cells. Lopez-Ramirez, M.A., McCurdy, S., Li, W. et al. FASEB Bioadv (2021) 3:334-355. DOI 10.1096/fba.2020-00141 · PubMed

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

4HDO 1.67 Å, Crystal structure of the binary Complex of KRIT1 bound to the Rap1 GTPase
4JIF 1.7 Å, Co-crystal structure of ICAP1 PTB domain in complex with a KRIT1 peptide
6OQ4 1.75 Å, Crystal Structure of the Ternary Complex of KRIT1 bound to both the Rap1 GTPase and HKi1
6OQ3 1.85 Å, Crystal Structure of the Ternary Complex of KRIT1 bound to both the Rap1 GTPase and HKi2
4DXA 1.95 Å, Co-crystal structure of Rap1 in complex with KRIT1
4HDQ 1.95 Å, Crystal Structure of the Ternary Complex of KRIT1 bound to both the Rap1 GTPase and the…
8SU8 2.01 Å, Co-crystal structure of KRIT1 with a 1-hydroxy 2-naphthaldehyde derivative…
8T09 2.15 Å, Co-crystal structure of KRIT1 with a 1-hydroxy 2-naphthaldehyde derivative…
8T7V 2.25 Å, Co-crystal structure of KRIT1 with a 1-hydroxy 2-naphthaldehyde derivative…
3U7D 2.49 Å, Crystal structure of the KRIT1/CCM1 FERM domain in complex with the heart of glass…
4DX8 2.54 Å, ICAP1 in complex with KRIT1 N-terminus
5D68 2.91 Å, Crystal structure of KRIT1 ARD-FERM

Browse structure collections

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