6AZ2: Asf1-Fab 12E complex

Crystal structure of Asf1-Fab 12E complex. Determined by X-ray diffraction at 2.48 Å resolution. Released 10 Jan 2018.

Method: X-ray diffraction
Resolution: 2.48 Å
Organisms: Homo sapiens, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 6
Atoms: 8,950
Mol. weight: 130.59 kDa
Released: 10 Jan 2018

Explore 6AZ2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6AZ2 contains 37 α-helices and 111 β-strands across 6 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: 6 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
β-strand	10-12	3	2
β-strand	18-25	8	1
α-helix	29-31	3
β-strand	33-39	7	2
β-strand	45-51	7	2
β-strand	58-60	3	2
β-strand	68-73	6	1
α-helix	74-76	3
β-strand	78-83	6	1
α-helix	88-90	3
β-strand	92-99	8	2
β-strand	108-109	2	2
β-strand	113-117	5	2
β-strand	122	1	3
β-strand	125-129	5	4
β-strand	140-150	11	4
β-strand	151	1	3
β-strand	156-159	4	5
β-strand	164	1	5
β-strand	168-170	3	4
α-helix	171-173	3
β-strand	174-175	2	4
β-strand	181-190	10	4
α-helix	191-193	3
β-strand	194	1	6
β-strand	197	1	6
β-strand	199-205	7	5
α-helix	206-208	3
β-strand	210-216	7	5

Chain B: 5 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	13
β-strand	16-17	2	14
α-helix	21	1
β-strand	22-30	9	13
β-strand	38-45	8	14
β-strand	55-62	8	14
α-helix	65-66	2
β-strand	68-76	9	13
α-helix	77-78	2
β-strand	92-101	10	14
β-strand	104-117	14	14
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	14
β-strand	145-148	4	14

Chain C: 6 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	7
β-strand	10-12	3	8
β-strand	18-25	8	7
α-helix	29-31	3
β-strand	33-39	7	8
β-strand	45-51	7	8
β-strand	58-60	3	8
β-strand	68-73	6	7
β-strand	78-83	6	7
α-helix	88-90	3
β-strand	92-99	8	8
β-strand	108-109	2	8
β-strand	113-117	5	8
β-strand	122	1	9
α-helix	123-124	2
β-strand	125-129	5	10
β-strand	140-150	11	10
β-strand	151	1	9
β-strand	156-159	4	11
β-strand	168-170	3	10
α-helix	171-173	3
β-strand	174-175	2	10
β-strand	181-190	10	10
α-helix	191-193	3
β-strand	194	1	12
β-strand	197	1	12
β-strand	199-205	7	11
α-helix	206-208	3
β-strand	210-216	7	11

Chain D: 6 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	4-11	8	15
β-strand	16-17	2	16
α-helix	21	1
β-strand	22-30	9	15
β-strand	38-45	8	16
β-strand	55-62	8	16
α-helix	65-66	2
β-strand	68-76	9	15
α-helix	77-80	4
α-helix	86-89	4
β-strand	92-101	10	16
β-strand	104-117	14	16
α-helix	120-124	5
α-helix	132-134	3
β-strand	135-139	5	16
β-strand	145-148	4	16

Chain E: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	6-9	4	17
β-strand	12-15	4	18
β-strand	21-27	7	17
β-strand	35-40	6	18
β-strand	47-51	5	18
β-strand	55-56	2	18
α-helix	57	1
β-strand	64-69	6	17
β-strand	72-77	6	17
α-helix	82-84	3
β-strand	86-92	7	18
β-strand	95	1	15
α-helix	98	1
β-strand	99-100	2	18
β-strand	104-108	5	18
β-strand	113	1	19
β-strand	116-120	5	20
α-helix	125-128	4
β-strand	131-141	11	20
β-strand	142	1	19
β-strand	146-152	7	21
β-strand	155-156	2	21
α-helix	157	1
β-strand	161-165	5	20
β-strand	175-184	10	20
α-helix	185-190	6
β-strand	194-200	7	21
β-strand	207-211	5	21

Chain F: 8 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	6-9	4	22
β-strand	12-15	4	23
β-strand	21-27	7	22
β-strand	35-40	6	23
β-strand	47-51	5	23
β-strand	55-56	2	23
α-helix	57	1
β-strand	64-69	6	22
β-strand	72-77	6	22
α-helix	82-84	3
β-strand	87-92	6	23
β-strand	95	1	13
α-helix	98	1
β-strand	99-100	2	23
β-strand	104-108	5	23
β-strand	113	1	24
α-helix	114-115	2
β-strand	116-120	5	25
α-helix	121-123	3
α-helix	124-127	4
β-strand	131-141	11	25
β-strand	142	1	24
β-strand	146-152	7	26
β-strand	155-156	2	26
β-strand	161-165	5	25
α-helix	166-169	4
β-strand	175-184	10	25
α-helix	185-190	6
β-strand	193-200	8	26
β-strand	207-212	6	26

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fab Heavy Chain	A, C	protein	229	Homo sapiens
Histone chaperone ASF1	B, D	protein	154	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P32447 (AlphaFold model)
Fab Light Chain	E, F	protein	215	Homo sapiens

Sequence of entity 1 (A, C), FASTA

>6AZ2_1 Fab Heavy Chain (chains A, C)
EISEVQLVESGGGLVQPGGSLRLSCAASGFNVSYSSIHWVRQAPGKGLEWVAYIYPSSGY
TSYADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARSYSTKLAMDYWGQGTLVTV
FNQIKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQS
SGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT

Sequence of entity 2 (B, D), FASTA

>6AZ2_2 Histone chaperone ASF1 (chains B, D)
GSIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSI
LVGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEE
ELRENPPAKVQVDHIVRNILAEKPRVTRFNIVWD

Sequence of entity 3 (E, F), FASTA

>6AZ2_3 Fab Light Chain (chains E, F)
SDIQMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVP
SRFSGSRSGTDFTLTISSLQPEDFATYYCQQSQWYPITFGQGTKVEIKRTVAAPSVFIFP
PSDSQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTL
TLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Primary citation

Locking the Elbow: Improved Antibody Fab Fragments as Chaperones for Structure Determination. Bailey, L.J., Sheehy, K.M., Dominik, P.K. et al. J Mol Biol (2018) 430:337-347. DOI 10.1016/j.jmb.2017.12.012 · PubMed

Other PDB entries of the same protein (UniProt P32447 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1ROC 1.5 Å, Crystal structure of the histone deposition protein Asf1
5UCB 1.52 Å, Structure of antigen-Fab complex with engineered switch residue region.
2HUE 1.7 Å, Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4
5UEK 1.7 Å, Structure of antigen-Fab 12E complex with Histone chaperone ASF1
5UEA 1.7 Å, Structure of antigen-Fab complex with Histone chaperone ASF1
6AYZ 2.1 Å, Crystal structure of Asf1-Fab 12E complex
2IDC 2.2 Å, Structure of the Histone H3-Asf1 Chaperone Interaction
4ZBJ 2.25 Å, UBN1 peptide bound to H3.3/H4/Asf1
4EO5 2.35 Å, Yeast Asf1 bound to H3/H4G94P mutant
5EII 2.44 Å, Structural determination of an protein complex of a Fab with increased solubility
4RRP 2.79 Å, Crystal Structure of the Fab complexed with antigen Asf1p, Northeast Structural Genomics…
9AWE 2.8 Å, The crystal structure of an engineered Protein GF with Human Kappa Fab

Browse structure collections

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