5D68: KRIT1 ARD-FERM

Crystal structure of KRIT1 ARD-FERM. Determined by X-ray diffraction at 2.91 Å resolution. Released 21 Oct 2015.

Method: X-ray diffraction
Resolution: 2.91 Å
Organism: Homo sapiens
Chains: 3
Atoms: 10,652
Mol. weight: 168.46 kDa
Released: 21 Oct 2015

Explore 5D68 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5D68 contains 81 α-helices and 36 β-strands across 3 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: 26 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	291-297	7
α-helix	301-309	9
α-helix	324-330	7
α-helix	334-342	9
α-helix	358-364	7
α-helix	368-376	9
α-helix	392-399	8
α-helix	404-412	9
α-helix	418-420	3
β-strand	421-425	5	1
β-strand	431-435	5	1
α-helix	439-441	3
α-helix	444-450	7
α-helix	455-458	4
β-strand	461-467	7	1
β-strand	470-473	4	1
α-helix	474-475	2
α-helix	480-485	6
α-helix	487-494	8
α-helix	499-501	3
β-strand	505-510	6	1
α-helix	516-519	4
α-helix	525-541	17
α-helix	548-563	16
α-helix	568-571	4
α-helix	578-581	4
α-helix	587-589	3
α-helix	594-596	3
α-helix	598-609	12
α-helix	618-630	13
β-strand	638-644	7	2
β-strand	656-662	7	2
β-strand	666-671	6	2
β-strand	677-682	6	2
β-strand	686-690	5	2
β-strand	696-701	6	2
β-strand	707-711	5	2
α-helix	715-727	13

Chain B: 28 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	291-298	8
α-helix	301-309	9
α-helix	324-330	7
α-helix	334-342	9
α-helix	350-352	3
α-helix	358-364	7
α-helix	368-376	9
α-helix	392-399	8
α-helix	404-412	9
α-helix	418-419	2
β-strand	420-425	6	3
β-strand	431-436	6	3
α-helix	439-441	3
α-helix	444-450	7
α-helix	455-458	4
β-strand	461-467	7	3
β-strand	470-473	4	3
α-helix	474-475	2
α-helix	480-485	6
α-helix	487-494	8
α-helix	499-501	3
β-strand	505-510	6	3
α-helix	516-519	4
α-helix	525-541	17
α-helix	548-563	16
α-helix	568-571	4
α-helix	578-581	4
α-helix	587-589	3
α-helix	594-596	3
α-helix	598-609	12
α-helix	618-630	13
β-strand	638-644	7	4
β-strand	656-662	7	4
β-strand	666-671	6	4
β-strand	677-682	6	4
β-strand	686-690	5	4
β-strand	696-701	6	4
β-strand	707-711	5	4
α-helix	715-727	13
α-helix	731-733	3

Chain C: 27 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	291-298	8
α-helix	301-309	9
α-helix	324-330	7
α-helix	334-342	9
α-helix	350-352	3
α-helix	358-364	7
α-helix	368-376	9
α-helix	392-399	8
α-helix	404-412	9
α-helix	418-419	2
β-strand	420-425	6	5
β-strand	431-436	6	5
α-helix	439-441	3
α-helix	444-450	7
α-helix	455-458	4
β-strand	461-467	7	5
β-strand	470-473	4	5
α-helix	474-475	2
α-helix	480-485	6
α-helix	487-494	8
α-helix	499-501	3
β-strand	505-510	6	5
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	587-589	3
α-helix	594-596	3
α-helix	598-609	12
α-helix	618-630	13
β-strand	638-644	7	6
β-strand	656-662	7	6
β-strand	666-671	6	6
β-strand	677-682	6	6
β-strand	686-690	5	6
β-strand	696-701	6	6
β-strand	707-711	5	6
α-helix	715-727	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Krev interaction trapped protein 1	A, B, C	protein	486	Homo sapiens	O00522 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>5D68_1 Krev interaction trapped protein 1 (chains A, B, C)
GSDILQGTDYSKIQIPKQEKWQRSMSSVTEDKERQWVDDFPLHRSACEGDSELLSRLLSE
RFSVNQLDSDHWAPIHYACWYGKVEATRILLEKGKCNPNLLNGQLSSPLHFAAGGGHAEI
VQILLNHPETDRHITDQQGRSPLNICEENKQNNWEEAAKLLKEAINKPYEKVRIYRMDGS
YRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHVRDWPEI
LAELTNLDPQRETPQLFLRRDVRLPLEVEKQIEDPLAILILFDEARYNLLKGFYTAPDAK
LITLASLLLQIVYGNYESKKHKQGFLNEENLKSIVPVTKLKSKAPHWTNRILHEYKNLST
SEGVSKEMHHLQRMFLQNCWEIPTYGAAFFTGQIFTKASPSNHKVIPVYVGVNIKGLHLL
NMETKALLISLKYGCFMWQLGDTDTCFQIHSMENKMSFIVHTKQAGLVVKLLMKLNGQLM
PTERNS

Primary citation

Structural analysis of the KRIT1 ankyrin repeat and FERM domains reveals a conformationally stable ARD-FERM interface. Zhang, R., Li, X., Boggon, T.J. J Struct Biol (2015) 192:449-456. DOI 10.1016/j.jsb.2015.10.006 · 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
6UZK 1.92 Å, Crystal Structure of the Ternary Complex of KRIT1 bound to both the Rap1 GTPase and HKi6
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

Browse structure collections

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