5WCI: Human MYST histone acetyltransferase 1

Name: PDB 5WCI: Human MYST histone acetyltransferase 1
Published: 2017-07-26
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: transferase

Human MYST histone acetyltransferase 1. Determined by X-ray diffraction at 1.78 Å resolution. Released 26 Jul 2017.

Method: X-ray diffraction
Resolution: 1.78 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,704
Mol. weight: 35.63 kDa
Ligands: ZN, 1VU
Released: 26 Jul 2017

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

Secondary structure: helices and β-sheets

5WCI contains 15 α-helices and 16 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: 15 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	168-170	3
α-helix	173-175	3
α-helix	177-179	3
β-strand	181-184	4	1
β-strand	187-190	4	1
α-helix	199-202	4
β-strand	207-209	3	1
β-strand	216-217	2	1
α-helix	220-229	10
β-strand	238-243	6	2
β-strand	246-252	7	2
α-helix	257-268	12
β-strand	283-291	9	2
β-strand	296-305	10	2
β-strand	312-314	3	3
β-strand	316-319	4	2
α-helix	321-323	3
α-helix	328-342	15
β-strand	347	1	4
β-strand	348-349	2	3
α-helix	350	1
α-helix	353-354	2
α-helix	355-375	21
α-helix	382-389	8
β-strand	391	1	4
α-helix	393-402	10
β-strand	406-409	4	5
β-strand	412-415	4	5
α-helix	419-427	9
α-helix	440-442	3
β-strand	443	1	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Histone acetyltransferase KAT8	A	protein	295	Homo sapiens	Q9H7Z6 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>5WCI_1 Histone acetyltransferase KAT8 (chains A)
MGSSHHHHHHSSGLVPRGSTKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCL
KYMKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVHEVDGKDHKIYCQNLCLLAKLFLDHK
TLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIA
FSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLENLRDFRGTLSIKDLSQMTSITQN
DIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSVCLKWAPPK

Ligands and cofactors

ID	Name	Formula	Copies
ZN	Zinc ion	Zn	1
1VU	propionyl Coenzyme A	C24 H40 N7 O17 P3 S	1

Water and common crystallization additives (EDO, CL) are not listed.

Primary citation

Human MYST histone acetyltransferase 1. Zeng, H., Dong, A., Walker, J.R. et al. To be published.

Other PDB entries of the same protein (UniProt Q9H7Z6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

29UU 1.3 Å, KAT8 mutant (KAT6A surrogate, myst-cryst) in complex with KAT6A inhibitor example-41
9OOA 1.39 Å, Crystal structure of MYST acetyltransferase domain in complex with inhibitor 7
29UT 1.4 Å, KAT8 mutant (KAT6A surrogate, myst-cryst) in complex with KAT6A inhibitor compound 2
2PQ8 1.45 Å, MYST histone acetyltransferase 1
9OOF 1.68 Å, Crystal structure of MYST acetyltransferase domain in complex with inhibitor 10e
29TM 1.7 Å, KAT8 mutant (KAT6A surrogate, myst-cryst) in complex with KAT6A inhibitor bay-7728
6OIN 1.7 Å, Crystal structure of MYST acetyltransferase domain in complex with inhibitor CTX-124143
6OIO 1.7 Å, Crystal structure of MYST acetyltransferase domain in complex with inhibitor 60
6OIQ 1.75 Å, Crystal structure of MYST acetyltransferase domain in complex with inhibitor 63
6OWI 1.75 Å, Crystal structure of MYST acetyltransferase domain in complex with inhibitor 85
29TN 1.8 Å, KAT8 mutant (KAT6A surrogate, myst-cryst) in complex with KAT6A inhibitor compound 38
6OIP 1.8 Å, Crystal structure of MYST acetyltransferase domain in complex with inhibitor 34

Browse structure collections

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