6TWQ: MAGI1_2

MAGI1_2 complexed with a 16E6 peptide. Determined by X-ray diffraction at 2.65 Å resolution. Released 1 Apr 2020.

Method: X-ray diffraction
Resolution: 2.65 Å
Organisms: Homo sapiens, Human papillomavirus type 16
Chains: 4
Atoms: 6,883
Mol. weight: 99.87 kDa
Ligands: CA, CIT
Released: 1 Apr 2020

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

Secondary structure: helices and β-sheets

6TWQ contains 49 α-helices and 18 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: 24 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	463-465	3
β-strand	469-476	8	3
β-strand	478-479	2	4
β-strand	481	1	4
β-strand	484-488	5	3
β-strand	496-501	6	3
α-helix	506-510	5
β-strand	518-522	5	3
β-strand	525-526	2	3
α-helix	532-541	10
α-helix	543	1
β-strand	547-554	8	3
α-helix	574-586	13
α-helix	592-599	8
α-helix	604-618	15
α-helix	622-627	6
α-helix	632-641	10
α-helix	645-655	11
α-helix	664-673	10
α-helix	676-690	15
α-helix	694-701	8
α-helix	705-714	10
α-helix	718-720	3
α-helix	727-739	13
α-helix	749-758	10
α-helix	761-771	11
α-helix	779-786	8
α-helix	789-817	29
α-helix	824-833	10
α-helix	839-850	12
α-helix	854-861	8
α-helix	864-874	11

Chain B: 25 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	463-465	3
β-strand	469-476	8	1
β-strand	478	1	2
β-strand	481	1	2
β-strand	484-488	5	1
β-strand	496-501	6	1
α-helix	506-510	5
β-strand	518-522	5	1
β-strand	525-526	2	1
α-helix	532-541	10
α-helix	543	1
β-strand	547-554	8	1
α-helix	574-586	13
α-helix	592-599	8
α-helix	604-618	15
α-helix	622-629	8
α-helix	632-641	10
α-helix	645-655	11
α-helix	664-673	10
α-helix	676-690	15
α-helix	694-701	8
α-helix	705-714	10
α-helix	718-720	3
α-helix	727-739	13
α-helix	749-758	10
α-helix	761-770	10
α-helix	771-773	3
α-helix	779-786	8
α-helix	789-818	30
α-helix	824-833	10
α-helix	839-850	12
α-helix	854-861	8
α-helix	864-874	11

Chains C and D: 0 helices, 1 β-strand

Element	Residues	Length	Sheet
β-strand	155-157	3	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1,Annexin A2	A, B	protein	427	Homo sapiens	H7C535, P07355 (AlphaFold model)
Thr-arg-arg-glu-thr-gln-leu	C, D	protein	10	Human papillomavirus type 16	P03126 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>6TWQ_1 Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1,Annexin A2 (chains A, B)
GSMGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDG
KMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLGSSAYGSVKAYTN
FDAERDALNIETAIKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALS
GHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYK
TDLEKDIISDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPK
WISIMTERSVPHLQKVFDRYKSYSPYDMLESIRKEVKGDLENAFLNLVQCIQNKPLYFAD
RLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKRKYGKSLYYYIQQDTKGDYQKALL
YLCGGDD

Sequence of entity 2 (C, D), FASTA

>6TWQ_2 THR-ARG-ARG-GLU-THR-GLN-LEU (chains C, D)
SSRTRRETQL

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	11
CIT	Citric acid	C6 H8 O7	3

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

Primary citation

Dual Specificity PDZ- and 14-3-3-Binding Motifs: A Structural and Interactomics Study. Gogl, G., Jane, P., Caillet-Saguy, C. et al. Structure (2020) 28:747-759.e3. DOI 10.1016/j.str.2020.03.010 · PubMed

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