1BFO: Campath-1G IGG2B rat monoclonal FAB

Name: PDB 1BFO: Campath-1G IGG2B rat monoclonal FAB
Published: 1999-03-16
License: https://creativecommons.org/publicdomain/zero/1.0/
Keywords: antibody

Campath-1G IGG2B rat monoclonal FAB. Determined by X-ray diffraction at 2.6 Å resolution. Released 16 Mar 1999.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Rattus rattus
Chains: 8
Atoms: 13,523
Mol. weight: 187.15 kDa
Released: 16 Mar 1999

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

Secondary structure: helices and β-sheets

1BFO contains 58 α-helices and 180 β-strands across 8 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: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
β-strand	5-7	3	1
β-strand	10-13	4	2
β-strand	19-24	6	1
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	85-90	6	2
α-helix	96	1
β-strand	97-98	2	2
β-strand	102-106	5	2
β-strand	111	1	3
α-helix	112-113	2
β-strand	114-118	5	4
α-helix	119-121	3
α-helix	122-125	4
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	158-162	5	4
α-helix	164-166	3
β-strand	172-181	10	4
α-helix	182-186	5
β-strand	190-196	7	5
β-strand	198-199	2	6
β-strand	201	1	6
β-strand	205-210	6	5

Chains B and H: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	7
β-strand	11-12	2	8
β-strand	18-25	8	7
α-helix	29-31	3
β-strand	34-39	6	9
β-strand	46-51	6	9
β-strand	60-62	3	9
β-strand	70-74	5	7
α-helix	76-78	3
β-strand	80-85	6	7
α-helix	90-92	3
β-strand	94-100	7	9
β-strand	110-111	2	9
β-strand	115-117	3	9
β-strand	118-119	2	8
β-strand	125	1	10
β-strand	128-132	5	11
β-strand	144-153	10	11
β-strand	154	1	10
β-strand	159-162	4	12
α-helix	163-165	3
β-strand	171-173	3	11
α-helix	174-176	3
β-strand	177-179	3	11
β-strand	182-191	10	11
β-strand	200-205	6	12
α-helix	206-208	3
β-strand	210-215	6	12

Chains C and E: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	13
β-strand	10-14	5	14
β-strand	19-24	6	13
β-strand	33-38	6	14
β-strand	45-49	5	14
β-strand	53-54	2	14
α-helix	55	1
β-strand	62-67	6	13
β-strand	70-75	6	13
α-helix	80-82	3
β-strand	84-90	7	14
α-helix	96	1
β-strand	97-98	2	14
β-strand	102-107	6	14
β-strand	111	1	15
α-helix	112-113	2
β-strand	114-118	5	16
α-helix	119-121	3
α-helix	122-125	4
β-strand	129-139	11	16
β-strand	140	1	15
β-strand	145-150	6	17
β-strand	153-154	2	17
β-strand	158-162	5	16
α-helix	164-166	3
β-strand	172-181	10	16
α-helix	182-186	5
β-strand	190-196	7	17
β-strand	198-199	2	18
β-strand	201	1	18
β-strand	205-210	6	17

Chain D: 7 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	19
β-strand	11-12	2	20
β-strand	18-25	8	19
α-helix	29-31	3
β-strand	34-39	6	21
β-strand	46-51	6	21
β-strand	60-62	3	21
β-strand	70-74	5	19
α-helix	76-78	3
β-strand	80-85	6	19
α-helix	90-92	3
β-strand	94-100	7	21
β-strand	110-111	2	21
β-strand	115-117	3	21
β-strand	118-119	2	20
β-strand	125	1	22
α-helix	126-127	2
β-strand	128-132	5	23
β-strand	143-153	11	23
β-strand	154	1	22
β-strand	159-162	4	24
α-helix	163-165	3
β-strand	171-173	3	23
α-helix	174-176	3
β-strand	177-179	3	23
β-strand	182-192	11	23
β-strand	200-205	6	24
α-helix	206-208	3
β-strand	210-215	6	24

Chain F: 6 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	31
β-strand	11-12	2	32
β-strand	18-25	8	31
α-helix	29-31	3
β-strand	34-39	6	33
β-strand	46-51	6	33
β-strand	60-62	3	33
β-strand	70-74	5	31
α-helix	76-78	3
β-strand	80-85	6	31
α-helix	90-92	3
β-strand	94-100	7	33
β-strand	110-111	2	33
β-strand	115-117	3	33
β-strand	118-119	2	32
β-strand	125	1	34
β-strand	128-132	5	35
β-strand	143-153	11	35
β-strand	154	1	34
β-strand	159-162	4	36
α-helix	163-165	3
β-strand	171-173	3	35
α-helix	174-176	3
β-strand	177-179	3	35
β-strand	182-192	11	35
β-strand	200-205	6	36
α-helix	206-208	3
β-strand	210-215	6	36

Chain G: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	37
β-strand	10-13	4	38
β-strand	19-24	6	37
β-strand	33-38	6	38
β-strand	45-49	5	38
β-strand	53-54	2	38
α-helix	55	1
β-strand	62-67	6	37
β-strand	70-75	6	37
α-helix	80-82	3
β-strand	85-90	6	38
α-helix	96	1
β-strand	97-98	2	38
β-strand	102-106	5	38
β-strand	111	1	39
α-helix	112-113	2
β-strand	114-118	5	40
α-helix	119-121	3
α-helix	122-125	4
β-strand	129-139	11	40
β-strand	140	1	39
β-strand	145-150	6	41
β-strand	153-154	2	41
β-strand	158-162	5	40
α-helix	164-166	3
β-strand	172-181	10	40
α-helix	182-186	5
β-strand	190-196	7	41
β-strand	198-199	2	42
β-strand	201	1	42
β-strand	205-210	6	41

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Campath-1G antibody	A, C, E, G	protein	214	Rattus rattus	P01835 (AlphaFold model)
Campath-1G antibody	B, D, F, H	protein	216	Rattus rattus	P20761 (AlphaFold model)

Sequence of entity 1 (A, C, E, G), FASTA

>1BFO_1 CAMPATH-1G ANTIBODY (chains A, C, E, G)
DIKMTQSPSFLSASVGDRVTLNCKASQNIDKYLNWYQQKLGESPKLLIYNTNNLQTGIPS
RFSGSGSGTDFTLTISSLQPEDVATYFCLQHISRPRTFGTGTKLELKRANAAPTVSIFPP
STEQLATGGASVVCLMNKFYPRDISVKWKIDGTERNGVLNSVTDQDSADSTYSMSSTLSL
TKADYQSHNLYTCQVVHKTSSSPVVAKNFNRNEC

Sequence of entity 2 (B, D, F, H), FASTA

>1BFO_2 CAMPATH-1G ANTIBODY (chains B, D, F, H)
EVKLLESGGGLVQPGGSMRLSCAGSGFTFTDFYMNWIRQPAGKAPEWLGFIRDKAKGYTT
EYNPSVKGRFTISRDNTQNMLYLQMNTLRAEDTATYYCAREGHTAAPFDYWGQGVMVTVS
SAQTTAPSVYPLAPGCGDTTSSTVTLGCLVKGYFPEPVTVTWNSGALSSDVHTFPAVLQS
GLYTLTSSVTSSTWPSQTVTCNVAHPASSTKVDKKV

Primary citation

Crystal structures of a rat anti-CD52 (CAMPATH-1) therapeutic antibody Fab fragment and its humanized counterpart. Cheetham, G.M., Hale, G., Waldmann, H. et al. J Mol Biol (1998) 284:85-99. DOI 10.1006/jmbi.1998.2157 · PubMed

Other PDB entries of the same protein (UniProt P01835 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1LK3 1.91 Å, Engineered human interleukin-10 monomer complexed to 9D7 FAB fragment
1C5D 2.4 Å, The crystal structure of the FAB fragment of a rat monoclonal antibody against the main…
1FN4 2.8 Å, Crystal structure of FAB198, an efficient protector of acetylcholine receptor against…
4UAO 3.1 Å, Crystal structure of Apical Membrane Antigen 1 from Plasmodium Knowlesi in complex with…

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