5LKT: PDB entry 5LKT

Crystal structure of the p300 acetyltransferase catalytic core with butyryl-coenzyme A. Determined by X-ray diffraction at 2.04 Å resolution. Released 2 Nov 2016.

Method
X-ray diffraction
Resolution
2.04 Å
Organism
Homo sapiens
Chains
1
Atoms
4,960
Mol. weight
68.59 kDa
Ligands
BCO, ZN
Released
2 Nov 2016

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

Secondary structure: helices and β-sheets

5LKT contains 36 α-helices and 19 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: 36 helices, 19 β-strands

ElementResiduesLengthSheet
α-helix1051-106616
α-helix1073-10753
α-helix1089-10924
α-helix1099-11079
α-helix1114-113118
α-helix1137-115923
β-strand116911
α-helix1170-11745
β-strand1175-117622
β-strand1184-118522
β-strand1190-119453
β-strand1198-120143
α-helix1202-12076
β-strand1212-121544
β-strand1224-122744
α-helix1228-12303
β-strand1232-123543
α-helix12401
β-strand124111
α-helix1242-12432
β-strand1244-124635
β-strand1253-125535
α-helix1256-12594
α-helix1273-12786
α-helix1283-12853
α-helix1294-12952
α-helix1297-131317
β-strand1321-1334146
α-helix1335-13362
α-helix1337-13393
α-helix1340-13445
β-strand1352-1366156
β-strand1369-1381136
α-helix13861
β-strand1392-140096
α-helix1407-14093
α-helix1410-142819
β-strand1432-143656
α-helix1439-14413
α-helix1456-14594
α-helix1460-147617
β-strand1482-148546
α-helix1486-14927
α-helix1498-15003
α-helix1508-151912
α-helix1584-15907
α-helix1592-15943
β-strand1595-159956
α-helix1603-16075
α-helix1609-16124
α-helix1617-16182
β-strand161916
α-helix1622-16243
α-helix1628-16369
α-helix1644-166118

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Histone acetyltransferase p300,Histone acetyltransferase p300Aprotein578Homo sapiensQ09472 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5LKT_1 Histone acetyltransferase p300,Histone acetyltransferase p300 (chains A)
GAMAGKAVPMQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDI
VKSPMDLSTIKRKLDTGQYQEPWQYVDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQE
IDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGES
VSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEIIWPAGFVC
DGCLKKSARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKT
VEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRR
VYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHP
PDQKIPKPKRLQEWFKKMLDKAVSERIVHDYKDIFKQATEDRLTSAKELPYFEGDFWPNV
LEESIKESGGSGSQKLYATMEKHKEVFFVIRLIAGPAANSLPPIVDPDPLIPCDLMDGRD
AFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRF

Ligands and cofactors

IDNameFormulaCopies
BCOButyryl Coenzyme AC25 H42 N7 O17 P3 S1
ZNZinc ionZn4

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

Primary citation

Structure of p300 in complex with acyl-CoA variants. Kaczmarska, Z., Ortega, E., Goudarzi, A. et al. Nat Chem Biol (2017) 13:21-29. DOI 10.1038/nchembio.2217 · PubMed

Other PDB entries of the same protein (UniProt Q09472 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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