6CZO: The KNL1-PP1 Holoenzyme

The KNL1-PP1 Holoenzyme. Determined by X-ray diffraction at 2.95 Å resolution. Released 23 Jan 2019.

Method: X-ray diffraction
Resolution: 2.95 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,075
Mol. weight: 82.63 kDa
Ligands: MN, PO4
Released: 23 Jan 2019

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

Secondary structure: helices and β-sheets

6CZO contains 24 α-helices and 37 β-strands across 4 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: 11 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	32-48	17
β-strand	52-55	4	1
β-strand	59-62	4	2
β-strand	64	1	3
α-helix	69-79	11
β-strand	87-89	3	2
α-helix	100-113	14
β-strand	118-120	3	2
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	1
β-strand	169-172	4	1
α-helix	184-187	4
α-helix	200-206	7
β-strand	208-209	2	4
β-strand	216-218	3	4
β-strand	225-227	3	4
α-helix	229-238	10
β-strand	243-246	4	1
β-strand	255-258	4	1
β-strand	263-266	4	1
β-strand	267	1	3
α-helix	272-274	3
β-strand	280-285	6	2
β-strand	290-297	8	2

Chain B: 0 helices, 3 β-strands

Element	Residues	Length	Sheet
β-strand	27	1	1
β-strand	60-61	2	2
β-strand	64-69	6	2

Chain C: 13 helices, 16 β-strands

Element	Residues	Length	Sheet
α-helix	9-17	9
α-helix	23	1
α-helix	32-48	17
β-strand	52-55	4	5
β-strand	59-62	4	2
β-strand	64	1	6
α-helix	69-79	11
β-strand	87-89	3	2
α-helix	100-113	14
β-strand	118-120	3	2
α-helix	128-131	4
α-helix	136-143	8
α-helix	146-156	11
β-strand	162-165	4	5
β-strand	169-172	4	5
α-helix	184-187	4
α-helix	194-196	3
α-helix	200-206	7
β-strand	208-209	2	7
β-strand	216-218	3	7
β-strand	225-227	3	7
α-helix	229-238	10
β-strand	243-246	4	5
β-strand	255-258	4	5
β-strand	263-266	4	5
β-strand	267	1	6
α-helix	272-274	3
β-strand	280-285	6	2
β-strand	290-296	7	2

Chain D: 0 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	27	1	5
β-strand	60-64	5	2

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Serine/threonine-protein phosphatase PP1-alpha catalytic subunit	A, C	protein	299	Homo sapiens	P62136 (AlphaFold model)
CASC5 protein	B, D	protein	62	Homo sapiens	Q8NG31 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>6CZO_1 Serine/threonine-protein phosphatase PP1-alpha catalytic subunit (chains A, C)
GHMGSLNLDSIIGRLLEVQGSRPGKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKI
CGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL
RGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQ
SMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGAEVVAKFLHKHDL
DLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPAD

Sequence of entity 2 (B, D), FASTA

>6CZO_2 CASC5 protein (chains B, D)
GAMGHSSILKPPRSPLQDLRGGNETVQESNALRNKKNSRRVSFADTIKVFQTESHMKIVR
KS

Ligands and cofactors

ID	Name	Formula	Copies
MN	Manganese (II) ion	Mn	4
PO4	Phosphate ion	O4 P	2

Primary citation

KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive. Bajaj, R., Bollen, M., Peti, W. et al. Structure (2018) 26:1327-1336.e4. DOI 10.1016/j.str.2018.06.013 · PubMed

Other PDB entries of the same protein (UniProt P62136 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6ZEG 1.09 Å, Structure of PP1-IRSp53 chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)] bound to…
6ZEH 1.3 Å, Structure of PP1-spectrin alpha II chimera [PP1(7-304) + linker (G/S)x9 + spectrin alpha…
6ZEI 1.39 Å, Structure of PP1-IRSp53 S455E chimera [PP1(7-304) + linker (G/S)x9 + IRSp53(449-465)]…
6DNO 1.45 Å, Crystal structure of Protein Phosphatase 1 (PP1) bound to the muscle glycogen-targeting…
4MOV 1.45 Å, 1.45 A Resolution Crystal Structure of Protein Phosphatase 1
6OBR 1.5 Å, PP1 Y134A in complex with Microcystin LR
3E7A 1.63 Å, Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin Nodularin-R
3E7B 1.7 Å, Crystal Structure of Protein Phosphatase-1 Bound to the natural toxin inhibitor Tautomycin
8SW6 1.76 Å, Protein Phosphatase 1 in complex with PP1-specific Phosphatase targeting peptide…
6ZEJ 1.78 Å, Structure of PP1-Phactr1 chimera [PP1(7-304) + linker (SGSGS) + Phactr1(526-580)]
7T0Y 1.8 Å, The Ribosomal RNA Processing 1B Protein Phosphatase-1 Holoenzyme
6OBS 1.8 Å, PP1 Y134K

Browse structure collections

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