1CT8: Catalytic antibody 7C8 complex

Catalytic antibody 7C8 complex. Determined by X-ray diffraction at 2.2 Å resolution. Released 10 Nov 1999.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Mus musculus
Chains: 4
Atoms: 6,921
Mol. weight: 95.8 kDa
Ligands: TAA
Released: 10 Nov 1999

Explore 1CT8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CT8 contains 28 α-helices and 89 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: 6 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	1
β-strand	10-13	4	2
β-strand	19-25	7	1
β-strand	33-38	6	2
β-strand	45-49	5	2
β-strand	53-54	2	2
β-strand	62-67	6	1
β-strand	70-75	6	1
α-helix	80-82	3
β-strand	84-90	7	2
α-helix	96	1
β-strand	97-98	2	2
β-strand	102-106	5	2
β-strand	111	1	3
β-strand	114-118	5	4
α-helix	119-121	3
α-helix	122-126	5
β-strand	129-139	11	4
β-strand	140	1	3
β-strand	145-150	6	5
β-strand	153-154	2	5
β-strand	159-163	5	4
α-helix	165-167	3
β-strand	173-182	10	4
α-helix	183-187	5
β-strand	191-197	7	5
β-strand	199	1	6
β-strand	201	1	6
β-strand	205-210	6	5

Chain B: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	7
α-helix	7-9	3
β-strand	10-12	3	8
β-strand	18-25	8	7
β-strand	33-39	7	8
β-strand	45-52	8	8
β-strand	57-59	3	8
β-strand	67-72	6	7
α-helix	73-75	3
β-strand	77-82	6	7
α-helix	84-86	3
β-strand	88-95	8	8
β-strand	102-103	2	8
β-strand	107-111	5	8
α-helix	115-116	2
β-strand	117	1	9
α-helix	118-119	2
β-strand	120-124	5	10
β-strand	135-145	11	10
β-strand	146	1	9
β-strand	151-154	4	11
α-helix	155-157	3
β-strand	163-165	3	10
α-helix	166-168	3
β-strand	169-171	3	10
β-strand	174-184	11	10
β-strand	194-199	6	11
α-helix	200-202	3
β-strand	204-209	6	11

Chain C: 7 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	12
β-strand	10-13	4	13
β-strand	19-25	7	12
β-strand	33-38	6	13
β-strand	45-49	5	13
β-strand	53-54	2	13
α-helix	55	1
β-strand	62-67	6	12
β-strand	70-75	6	12
α-helix	80-82	3
β-strand	84-90	7	13
α-helix	96	1
β-strand	97-98	2	13
β-strand	102-106	5	13
β-strand	111	1	14
β-strand	114-118	5	15
α-helix	119-121	3
α-helix	122-126	5
β-strand	129-139	11	15
β-strand	140	1	14
β-strand	145-150	6	16
β-strand	153-154	2	16
β-strand	159-163	5	15
α-helix	165-167	3
β-strand	173-182	10	15
α-helix	183-186	4
β-strand	191-197	7	16
β-strand	199	1	17
β-strand	201	1	17
β-strand	205-210	6	16

Chain D: 7 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	18
α-helix	7-9	3
β-strand	10-12	3	19
β-strand	18-25	8	18
β-strand	33-39	7	19
β-strand	45-52	8	19
β-strand	57-59	3	19
β-strand	67-72	6	18
β-strand	77-82	6	18
α-helix	84-86	3
β-strand	88-95	8	19
β-strand	102-103	2	19
β-strand	104	1	18
β-strand	107-111	5	19
α-helix	115-116	2
β-strand	117	1	20
α-helix	118-119	2
β-strand	120-124	5	21
β-strand	135-145	11	21
β-strand	146	1	20
β-strand	151-154	4	22
α-helix	155-157	3
β-strand	163-165	3	21
α-helix	166-168	3
β-strand	169-171	3	21
β-strand	174-184	11	21
β-strand	193-199	7	22
α-helix	200-202	3
β-strand	204-210	7	22

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
7C8 FAB fragment; short chain	A, C	protein	214	Mus musculus	P01837 (AlphaFold model)
7C8 FAB fragment; long chain	B, D	protein	220	Mus musculus	P01868 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1CT8_1 7C8 FAB FRAGMENT; SHORT CHAIN (chains A, C)
ELVMTQTPATLSVTPGDSVSLSCRASQSVSNKLHWYQQKSHESPRLLIKFASQSIPGIPS
RFSGSGSGSDFTLSINSVETEDFGIYFCHQTHGRPLTFGAGTKLELKRADAAPTVSIFPP
SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT
LTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC

Sequence of entity 2 (B, D), FASTA

>1CT8_2 7C8 FAB FRAGMENT; LONG CHAIN (chains B, D)
QVKLLESGAVLVKPGASVKLSCKTSGFTFSSSYINWLKQKPGQSLEWIAWIYAGSGGTVY
NQHFTDKARLTVDTSSSTAYMQFSSLTTEDSAIYYCARYRYDEGFAYWGQGTLVTVSAAK
TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVPRDC

Ligands and cofactors

ID	Name	Formula	Copies
TAA	[4-(2,2,2-trifluoro-acetylamino)-benzyl]-phosphonic acid…	C20 H21 Cl2 F3 N3 O8 P	2

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

Primary citation

Diverse structural solutions to catalysis in a family of antibodies. Gigant, B., Tsumuraya, T., Fujii, I. et al. Structure (1999) 7:1385-1393. DOI 10.1016/S0969-2126(00)80028-3 · PubMed

Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3D9A 1.2 Å, High Resolution Crystal Structure Structure of HyHel10 Fab Complexed to Hen Egg Lysozyme
1RUR 1.5 Å, Crystal Structure (I) of native Diels-Alder antibody 13G5 Fab at pH 8.0 with a data set…
2AJU 1.5 Å, Cyrstal structure of cocaine catalytic antibody 7A1 Fab'
2AJV 1.5 Å, Crystal Structure of Cocaine catalytic Antibody 7A1 Fab' in Complex with Cocaine
2W60 1.5 Å, Anti citrullinated Collagen type 2 antibody acc4
2W9D 1.57 Å, Structure of Fab fragment of the ICSM 18 - anti-Prp therapeutic antibody at 1.57 A…
3BKJ 1.59 Å, Crystal structure of Fab wo2 bound to the n terminal domain of amyloid beta peptide (1-16)
3BAE 1.59 Å, Crystal structure of Fab WO2 bound to the N terminal domain of Amyloid beta peptide (1-28)
2R1Y 1.6 Å, Crystal structure of S25-2 Fab in complex with Kdo analogues
2R2B 1.6 Å, Crystal structure of S25-2 Fab in complex with Kdo analogues
3BKM 1.6 Å, Structure of anti-amyloid-beta Fab WO2 (Form A, P212121)
3CFB 1.6 Å, High-resolution structure of blue fluorescent antibody EP2-19G2 in complex with stilbene…

Browse structure collections

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