6L1P: PHF20L1

Crystal structure of PHF20L1 in complex with Hit 1. Determined by X-ray diffraction at 1.23 Å resolution. Released 23 Sept 2020.

Method: X-ray diffraction
Resolution: 1.23 Å
Organism: Homo sapiens
Chains: 4
Atoms: 2,879
Mol. weight: 36.1 kDa
Ligands: E3X
Released: 23 Sept 2020

Explore 6L1P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6L1P contains 10 α-helices and 26 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: 2 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	18-22	5	4
β-strand	28-37	10	4
β-strand	42-47	6	4
β-strand	50	1	3
α-helix	52-54	3
β-strand	56-59	4	4
β-strand	65-66	2	4
α-helix	67-69	3

Chain B: 3 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	4-7	4
β-strand	8	1	1
β-strand	11	1	1
β-strand	18-22	5	2
β-strand	28-37	10	2
β-strand	42-47	6	2
β-strand	50	1	3
α-helix	52-54	3
β-strand	56-59	4	2
β-strand	65-66	2	2
α-helix	67-69	3

Chain C: 3 helices, 5 β-strands

Element	Residues	Length	Sheet
α-helix	4-6	3
β-strand	18-22	5	5
β-strand	28-37	10	5
β-strand	42-47	6	5
α-helix	52-54	3
β-strand	56-59	4	5
β-strand	65-66	2	5
α-helix	67-69	3

Chain D: 2 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	7-8	2	6
β-strand	11-12	2	6
β-strand	18-22	5	7
β-strand	28-37	10	7
β-strand	42-47	6	7
α-helix	52-54	3
β-strand	56-59	4	7
β-strand	65-66	2	7
α-helix	67-69	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
PHD finger protein 20-like protein 1	A, B, C, D	protein	70	Homo sapiens	A8MW92 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>6L1P_1 PHD finger protein 20-like protein 1 (chains A, B, C, D)
GSHMPPNRPGITFEIGARLEALDYLQKWYPSRIEKIDYEEGKMLVHFERWSHRYDEWIYW
DSNRLRPLER

Ligands and cofactors

ID	Name	Formula	Copies
E3X	4-(1-methyl-3,6-dihydro-2H-pyridin-4-yl)phenol	C12 H15 N O	4

Water and common crystallization additives (SO4, GOL) are not listed.

Primary citation

Conformational Selection in Ligand Recognition by the First Tudor Domain of PHF20L1. Lv, M., Gao, J., Li, M. et al. J Phys Chem Lett (2020) 11:7932-7938. DOI 10.1021/acs.jpclett.0c02039 · PubMed

Other PDB entries of the same protein (UniProt A8MW92 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6L0X 1.3 Å, The First Tudor Domain of PHF20L1
21EE 1.34 Å, Crystal structure of human PHF20L1(1-80) in complex with H3K36me
6L1C 1.58 Å, Crystal Structure Of of PHF20L1 Tudor1 Y24L mutant
6L10 1.6 Å, PHF20L1 Tudor1 - MES
6L1I 1.85 Å, Crystal Structure Of of PHF20L1 Tudor1 Y24W/Y29W mutant
6L1F 1.9 Å, Crystal structure of PHF20L1 Tudor1 in complex with K142me1 DNMT1
21ED 2.31 Å, Crystal structure of human PHF20L1(85-142)
2EQM Solution structure of the TUDOR domain of PHD finger protein 20-like 1 [Homo sapiens]
2EQU Solution structure of the tudor domain of PHD finger protein 20-like 1
2JTF Solution Structure of the PHF20L1 MBT domain

Browse structure collections

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