5HZH: PDB entry 5HZH

Crystal structure of photoinhibitable Rac1 containing C450A mutant LOV2 domain. Determined by X-ray diffraction at 2.6 Å resolution. Released 21 Dec 2016.

Method: X-ray diffraction
Resolution: 2.6 Å
Organisms: Homo sapiens, Avena sativa
Chains: 1
Atoms: 2,622
Mol. weight: 38.15 kDa
Ligands: GTP, FMN, MG, CA
Released: 21 Dec 2016

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

Secondary structure: helices and β-sheets

5HZH contains 16 α-helices and 11 β-strands across 1 chain. 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: 16 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	1
α-helix	16-24	9
β-strand	37-45	9	1
β-strand	62-65	4	2
β-strand	74-77	4	2
α-helix	79-85	7
α-helix	89-92	4
α-helix	97-100	4
α-helix	107-118	12
β-strand	123-130	8	2
β-strand	136-147	12	2
β-strand	153-163	11	2
α-helix	169-195	27
β-strand	199-207	9	1
α-helix	211-213	3
α-helix	217-220	4
β-strand	226-232	7	1
α-helix	236-241	6
α-helix	242-246	5
α-helix	247-253	7
β-strand	259-264	6	1
α-helix	266-268	3
α-helix	272-279	8
α-helix	285-287	3
α-helix	288-297	10
β-strand	302-305	4	1
α-helix	314-326	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ras-related C3 botulinum toxin substrate 1,NPH1-1,Ras-related C3 botulinum toxin substrate 1	A	protein	332	Homo sapiens, Avena sativa	O49003 (AlphaFold model), P63000 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5HZH_1 Ras-related C3 botulinum toxin substrate 1,NPH1-1,Ras-related C3 botulinum toxin substrate 1 (chains A)
GGSMQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGSGLATTLER
IEKNFVITDPRLPDNPIIFASDSFLQLTEYSREEILGRNARFLQGPETDRATVRKIRDAI
DNQTEVTVQLINYTKSGKKFWNLFHLQPMRDQKGDVQYFIGVQLDGTEHVRDAAEREGVM
LIKKTAENIDEAAKELGSGGKPVNLGLWDTAGLEDYDRLRPLSYPQTDVFLICFSLVSPA
SFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKE
IGAVKYLECSALTQRGLKTVFDEAIRAVLCPP

Ligands and cofactors

ID	Name	Formula	Copies
GTP	Guanosine-5'-triphosphate	C10 H16 N5 O14 P3	1
FMN	Flavin mononucleotide	C17 H21 N4 O9 P	1
MG	Magnesium ion	Mg	1
CA	Calcium ion	Ca	2

Primary citation

Engineering extrinsic disorder to control protein activity in living cells. Dagliyan, O., Tarnawski, M., Chu, P.H. et al. Science (2016) 354:1441-1444. DOI 10.1126/science.aah3404 · PubMed

Other PDB entries of the same protein (UniProt O49003 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7PGZ 0.9 Å, Structure of dark-adapted AsLOV2 Q513L
7PH0 0.98 Å, Structure of light-adapted AsLOV2 Q513L
7PGX 1.0 Å, Structure of dark-adapted AsLOV2 wild type
7PGY 1.09 Å, Structure of light-adapted AsLOV2 wild type
2V0U 1.4 Å, n- and c-terminal helices of oat lov2 (404-546) are involved in light-induced signal…
2V1B 1.55 Å, N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal…
2WKQ 1.6 Å, Structure of a photoactivatable Rac1 containing the Lov2 C450A Mutant
2V1A 1.65 Å, N- and C-terminal helices of oat LOV2 (404-546) are involved in light-induced signal…
2V0W 1.7 Å, N- and C-terminal helices of oat LOV2 (404-546) are involved in light- induced signal…
6NTP 1.89 Å, PTP1B Domain of PTP1B-LOV2 Chimera
2WKP 1.9 Å, Structure of a photoactivatable Rac1 containing Lov2 Wildtype
4WF0 1.95 Å, Crystal Structure of iLID - an Improved Light-Inducible Dimer

Browse structure collections

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