2Z2R: Nucleosome assembly proteins I

Nucleosome assembly proteins I (NAP-1, 74-365). Determined by X-ray diffraction at 3.2 Å resolution. Released 11 Mar 2008.

Method: X-ray diffraction
Resolution: 3.2 Å
Organism: Saccharomyces cerevisiae
Chains: 2
Atoms: 4,468
Mol. weight: 67.76 kDa
Released: 11 Mar 2008

Explore 2Z2R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2Z2R contains 29 α-helices and 17 β-strands across 2 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: 15 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	83-86	4
α-helix	90-140	51
α-helix	144-146	3
α-helix	147-160	14
α-helix	166-168	3
α-helix	188-195	8
α-helix	197-200	4
α-helix	205-211	7
β-strand	214-217	4	1
β-strand	220-221	2	1
β-strand	228-235	8	1
β-strand	243	1	2
β-strand	247-254	8	1
α-helix	255	1
α-helix	258-259	2
β-strand	266-271	6	1
β-strand	276	1	2
β-strand	285-293	9	3
β-strand	300-308	9	3
α-helix	312-316	5
α-helix	333-346	14
α-helix	347-352	6
α-helix	353-355	3
α-helix	356-361	6

Chain B: 14 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	90-140	51
α-helix	144-146	3
α-helix	147-159	13
α-helix	163-165	3
α-helix	188-195	8
α-helix	197-200	4
α-helix	205-211	7
β-strand	214-222	9	4
β-strand	228-235	8	4
β-strand	243	1	5
β-strand	247-254	8	4
β-strand	266-271	6	4
β-strand	276	1	5
α-helix	279-281	3
β-strand	285-294	10	6
β-strand	299-308	10	6
α-helix	312-316	5
α-helix	318-320	3
α-helix	330-333	4
α-helix	336-347	12
α-helix	348-352	5
α-helix	356-361	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Nucleosome assembly protein	A, B	protein	292	Saccharomyces cerevisiae	P25293 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>2Z2R_1 Nucleosome assembly protein (chains A, B)
LGSLVGQDSGYVGGLPKNVKEKLLSLKTLQSELFEVEKEFQVEMFELENKFLQKYKPIWE
QRSRIISGQEQPKPEQIAKGQEIVESLNETELLVDEEEKAQNDSEEEQVKGIPSFWLTAL
ENLPIVCDTITDRDAEVLEYLQDIGLEYLTDGRPGFKLLFRFDSSANPFFTNDILCKTYF
YQKELGYSGDFIYDHAEGCEISWKDNAHNVTVDLEMRKQRNKTTKQVRTIEKITPIESFF
NFFDPPKIQNEDQDEELEEDLEERLALDYSIGEQLKDKLIPRAVDWFTGAAL

Primary citation

A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1. Park, Y.J., McBryant, S.J., Luger, K. J Mol Biol (2008) 375:1076-1085. DOI 10.1016/j.jmb.2007.11.031 · PubMed

Other PDB entries of the same protein (UniProt P25293 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9B3I 2.88 Å, Cryo-EM structure of yeast (Nap1)2-H2A-H2B-Kap114-RanGTP
2AYU 3.0 Å, The structure of nucleosome assembly protein suggests a mechanism for histone binding…
9B23 3.2 Å, Cryo-EM structure of Nap1 core
9B31 3.2 Å, Cryo-EM structure of yeast (Nap1)2-Kap114-H2A-H2B
9B3F 3.54 Å, Cryo-EM structure of yeast (Nap1)2-H2A-H2B-Kap114
5G2E 6.7 Å, Structure of the Nap1 H2A H2B complex

Browse structure collections

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