4Z5R: Rontalizumab Fab

Rontalizumab Fab bound to Interferon-a2. Determined by X-ray diffraction at 3.0 Å resolution. Released 8 Jul 2015.

Method: X-ray diffraction
Resolution: 3.0 Å
Organism: Homo sapiens
Chains: 24
Atoms: 34,056
Mol. weight: 540.25 kDa
Released: 8 Jul 2015

Explore 4Z5R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4Z5R contains 168 α-helices and 356 β-strands across 24 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, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	80
β-strand	10-13	4	81
β-strand	19-25	7	80
β-strand	27C	1	82
β-strand	31	1	82
β-strand	33-38	6	81
β-strand	45-49	5	81
β-strand	53-54	2	81
α-helix	55	1
β-strand	62-67	6	80
β-strand	70-75	6	80
α-helix	80-82	3
β-strand	84-90	7	81
β-strand	98	1	81
β-strand	102-106	5	81
β-strand	111	1	83
β-strand	114-118	5	84
α-helix	119-121	3
α-helix	122-126	5
β-strand	131-139	9	84
β-strand	140	1	83
β-strand	145-150	6	85
β-strand	153-154	2	85
β-strand	159-163	5	84
α-helix	164-167	4
β-strand	173-180	8	84
α-helix	183-186	4
β-strand	191-197	7	85
β-strand	205-210	6	85

Chain B: 5 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	86
β-strand	10-12	3	87
β-strand	18-25	8	86
α-helix	29-31	3
β-strand	33-39	7	87
β-strand	45-51	7	87
β-strand	57-59	3	87
α-helix	61-63	3
β-strand	68-72	5	86
β-strand	77-82	6	86
α-helix	84-86	3
β-strand	88-95	8	87
β-strand	97	1	88
β-strand	99	1	88
β-strand	102-103	2	87
β-strand	107-111	5	87
β-strand	117	1	89
β-strand	120-124	5	90
β-strand	135-145	11	90
β-strand	146	1	89
β-strand	151-154	4	91
β-strand	159	1	91
β-strand	164-165	2	90
α-helix	166-168	3
β-strand	169-170	2	90
β-strand	176-185	10	90
β-strand	195-200	6	91
α-helix	201-203	3
β-strand	205-210	6	91

Chain D: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	12-20	9
α-helix	26-28	3
α-helix	30-32	3
α-helix	40-42	3
α-helix	53-66	14
α-helix	70-75	6
α-helix	78-100	23
α-helix	112-133	22
α-helix	137-155	19

Chains E, F, H, I, N and X: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	12-20	9
α-helix	26-28	3
α-helix	30-32	3
α-helix	40-42	3
α-helix	53-66	14
α-helix	70-75	6
α-helix	78-100	23
α-helix	112-132	21
α-helix	137-155	19

Chain G: 9 helices, 0 β-strands

Element	Residues	Length
α-helix	12-20	9
α-helix	26-28	3
α-helix	30-32	3
α-helix	40-42	3
α-helix	53-66	14
α-helix	70-75	6
α-helix	78-100	23
α-helix	114-132	19
α-helix	137-155	19

Chain J: 6 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-14	5	2
β-strand	19-25	7	1
β-strand	27C	1	3
β-strand	31	1	3
β-strand	33-38	6	2
β-strand	45-49	5	2
β-strand	53-54	2	2
α-helix	55	1
β-strand	62-67	6	1
β-strand	70-75	6	1
α-helix	80-82	3
β-strand	84-90	7	2
β-strand	98	1	2
β-strand	102-107	6	2
β-strand	111	1	4
β-strand	114-118	5	5
α-helix	119-121	3
α-helix	122-126	5
β-strand	129-139	11	5
β-strand	140	1	4
β-strand	145	1	6
β-strand	148-150	3	7
β-strand	153-154	2	7
β-strand	159-163	5	5
α-helix	164-167	4
β-strand	173-182	10	5
α-helix	183-187	5
β-strand	191-196	6	7
β-strand	197	1	6
β-strand	205-210	6	7

Chain K: 7 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	8
β-strand	10-12	3	9
β-strand	18-25	8	8
α-helix	29-31	3
β-strand	33-39	7	9
β-strand	45-51	7	9
β-strand	57-59	3	9
α-helix	61-63	3
β-strand	68-72	5	8
β-strand	77-82	6	8
α-helix	84-86	3
β-strand	88-95	8	9
β-strand	97	1	10
β-strand	99	1	10
β-strand	102-103	2	9
β-strand	107-111	5	9
α-helix	115-116	2
β-strand	117	1	11
β-strand	120-124	5	12
β-strand	135-145	11	12
β-strand	146	1	11
β-strand	151-154	4	13
β-strand	163-165	3	12
α-helix	166-168	3
β-strand	169-170	2	12
β-strand	176-185	10	12
α-helix	186-188	3
β-strand	189	1	14
β-strand	192	1	14
β-strand	195-200	6	13
α-helix	201-203	3
β-strand	205-210	6	13

Chain L: 6 helices, 25 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	15
β-strand	10-14	5	16
β-strand	19-25	7	15
β-strand	27C	1	17
β-strand	31	1	17
β-strand	33-38	6	16
β-strand	45-49	5	16
β-strand	53-54	2	16
α-helix	55	1
β-strand	62-67	6	15
β-strand	70-75	6	15
α-helix	80-82	3
β-strand	84-90	7	16
β-strand	98	1	16
β-strand	102-107	6	16
β-strand	111	1	18
α-helix	112-113	2
β-strand	114-118	5	19
α-helix	119-121	3
α-helix	122-126	5
β-strand	129-139	11	19
β-strand	140	1	18
β-strand	145	1	20
β-strand	148-150	3	21
β-strand	153-154	2	21
β-strand	159-163	5	19
β-strand	173-182	10	19
α-helix	183-186	4
β-strand	191-196	6	21
β-strand	197	1	20
β-strand	205-210	6	21

11 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Interferon alpha-2	D, E, F, G, H, I, N, X	protein	165	Homo sapiens	P01563 (AlphaFold model)
anti-IFN-a antibody rontalizumab light chain	A, J, L, P, R, T, V, Y	protein	218	Homo sapiens
anti-IFN-a antibody rontalizumab heavy chain modules VH and CH1 (Fab)	B, K, M, Q, S, U, W, Z	protein	225	Homo sapiens

Sequence of entity 1 (D, E, F, G, H, I, N, X), FASTA

>4Z5R_1 Interferon alpha-2 (chains D, E, F, G, H, I, N, X)
CDLPQTHSLGSRRTLMLLAQMRKISLFSCLKDRHDFGFPQEEFGNQFQKAETIPVLHEMI
QQIFNLFSTKDSSAAWDETLLDKFYTELYQQLNDLEACVIQGVGVTETPLMKEDSILAVR
KYFQRITLYLKEKKYSPCAWEVVRAEIMRSFSLSTNLQESLRSKE

Sequence of entity 2 (A, J, L, P, R, T, V, Y), FASTA

>4Z5R_2 anti-IFN-a antibody rontalizumab light chain (chains A, J, L, P, R, T, V, Y)
DIQMTQSPSSLSASVGDRVTITCRASQSVSTSSYSYMHWYQQKPGKAPKVLISYASNLES
GVPSRFSGSGSGTDFTLTISSLQPEDFATYYCQHSWGIPRTFGQGTKVEIKRTVAAPSVF
IFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLS
STLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 3 (B, K, M, Q, S, U, W, Z), FASTA

>4Z5R_3 anti-IFN-a antibody rontalizumab heavy chain modules VH and CH1 (Fab) (chains B, K, M, Q, S, U, W, Z)
EVQLVESGGGLVQPGGSLRLSCATSGYTFTEYIIHWVRQAPGKGLEWVASINPDYDITNY
NQRFKGRFTISLDKSKRTAYLQMNSLRAEDTAVYYCASWISDFFDYWGQGTLVTVSSAST
KGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLY
SLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCDKTHT

Primary citation

Structural basis of the broadly neutralizing anti-interferon-alpha antibody rontalizumab. Maurer, B., Bosanac, I., Shia, S. et al. Protein Sci (2015) 24:1440-1450. DOI 10.1002/pro.2729 · PubMed

Other PDB entries of the same protein (UniProt P01563 (AlphaFold model), which also has an AlphaFold model), best resolution first:

9GVO 1.81 Å, type-I interferons autoantibodies pmab15 and pmab14 in complex with Interferon alpha-2
3S9D 2.0 Å, binary complex between IFNa2 and IFNAR2
9GVL 2.01 Å, type-I interferons autoantibody pmab15 in complex with Interferon alpha-2
1RH2 2.9 Å, Recombinant human interferon-alpha 2B
4YPG 3.0 Å, Structural Insights Into the Neutralization Properties of a Human Anti-Interferon…
9GW5 4.0 Å, type-I interferon autoantibodies pmab3, pmab19 and pmab14 in complex with Interferon…
3SE3 4.0 Å, human IFNa2-IFNAR ternary complex
1ITF Interferon alpha-2A, NMR, 24 structures
2HYM NMR based Docking Model of the Complex between the Human Type I Interferon Receptor and…
2KZ1 Inter-molecular interactions in a 44 kDa interferon-receptor complex detected by…
2LAG Structure of the 44 kDa complex of interferon-alpha2 with the extracellular part of…
2LMS A single GalNAc residue on Threonine-106 modifies the dynamics and the structure of…

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