5UCB: Fab Heavy Chain

Structure of antigen-Fab complex with engineered switch residue region. Determined by X-ray diffraction at 1.52 Å resolution. Released 27 Dec 2017.

Method: X-ray diffraction
Resolution: 1.52 Å
Organisms: Homo sapiens, Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Chains: 3
Atoms: 5,097
Mol. weight: 63.42 kDa
Released: 27 Dec 2017

Explore 5UCB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5UCB contains 23 α-helices and 57 β-strands across 3 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 B: 7 helices, 10 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	13
β-strand	15-16	2	14
α-helix	20	1
β-strand	21-29	9	13
β-strand	37-46	10	14
β-strand	51-61	11	14
α-helix	64-65	2
β-strand	67-75	9	13
α-helix	76-78	3
α-helix	80-82	3
α-helix	85-88	4
β-strand	91-100	10	14
β-strand	103-116	14	14
α-helix	119-123	5
α-helix	131-133	3
β-strand	134-138	5	14
β-strand	144-147	4	14

Chain H: 7 helices, 26 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	1
β-strand	11-12	2	2
β-strand	18-25	8	1
α-helix	29-31	3
β-strand	34-39	6	3
β-strand	45-51	7	3
β-strand	57-59	3	3
β-strand	67-72	6	1
β-strand	77-82	6	1
α-helix	84-86	3
β-strand	88-96	9	3
β-strand	99-103	5	3
β-strand	107-109	3	3
β-strand	110-111	2	2
β-strand	116	1	4
α-helix	118-119	2
β-strand	120-124	5	5
β-strand	131-132	2	5
β-strand	135-145	11	5
β-strand	146	1	4
β-strand	151-154	4	6
α-helix	155-157	3
β-strand	159	1	6
β-strand	163-165	3	5
α-helix	166-168	3
β-strand	169-170	2	5
β-strand	176-185	10	5
α-helix	186-188	3
β-strand	189	1	7
β-strand	192	1	7
β-strand	195-200	6	6
α-helix	201-203	3
β-strand	205-210	6	6

Chain L: 9 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	8
β-strand	10-13	4	9
β-strand	19-25	7	8
α-helix	30-32	3
β-strand	33-38	6	9
β-strand	45-49	5	9
β-strand	53-54	2	9
α-helix	55	1
β-strand	62-67	6	8
β-strand	70-75	6	8
α-helix	80-82	3
β-strand	85-91	7	9
β-strand	96-98	3	9
β-strand	102-106	5	9
β-strand	111	1	10
α-helix	112-113	2
β-strand	114-118	5	11
α-helix	119-121	3
α-helix	122-126	5
β-strand	129-139	11	11
β-strand	140	1	10
β-strand	145-150	6	12
β-strand	153-154	2	12
α-helix	155	1
β-strand	159-163	5	11
α-helix	164-167	4
β-strand	173-182	10	11
α-helix	183-187	5
β-strand	191-197	7	12
β-strand	205-210	6	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Fab Heavy Chain	H	protein	217	Homo sapiens
Fab Light Chain	L	protein	210	Homo sapiens
Histone chaperone ASF1	B	protein	153	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)	P32447 (AlphaFold model)

Sequence of entity 1 (H), FASTA

>5UCB_1 Fab Heavy Chain (chains H)
EVQLVESGGGLVQPGGSLRLSCAASGFNVSYYSIHWVRQAPGKGLEWVASIYPYYGSTSY
ADSVKGRFTISADTSKNTAYLQMNSLRAEDTAVYYCARGYGWALDYWGQGTLVTVFNQIK
PPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYS
LSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPK

Sequence of entity 2 (L), FASTA

>5UCB_2 Fab Light Chain (chains L)
QMTQSPSSLSASVGDRVTITCRASQSVSSAVAWYQQKPGKAPKLLIYSASSLYSGVPSRF
SGSRSGTDYTLTISSLQPEDFATYYCQQDGWSLITFGQGTKVEIKRTVAAPSVFIFPPSD
EQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLTLS
KADYEKHKVYACEVTHQGLSSPVTKSFNRG

Sequence of entity 3 (B), FASTA

>5UCB_3 Histone chaperone ASF1 (chains B)
SIVSLLGIKVLNNPAKFTDPYEFEITFECLESLKHDLEWKLTYVGSSRSLDHDQELDSIL
VGPVPVGVNKFVFSADPPSAELIPASELVSVTVILLSCSYDGREFVRVGYYVNNEYDEEE
LRENPPAKVQVDHIVRNILAEKPRVTRFNIVWD

Primary citation

Antibody Switch Residue Engineering for Improved Crystallization Chaperones. Bailey, L.J., Kossiakoff, A.A. To be published.

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
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
6AZ2 2.48 Å, Crystal structure of Asf1-Fab 12E complex
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

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