43C9: Protein)

Crystallographic structure of the esterolytic and amidolytic 43C9 antibody. Determined by X-ray diffraction at 2.2 Å resolution. Released 18 Aug 1999.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Mus musculus
Chains: 8
Atoms: 7,254
Mol. weight: 101.13 kDa
Released: 18 Aug 1999

Explore 43C9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

43C9 contains 21 α-helices and 99 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: 2 helices, 13 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	27C-27D	2	3
β-strand	30-31	2	3
β-strand	33-38	6	2
β-strand	44-49	6	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	102-106	5	2

Chain B: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	4
β-strand	10-12	3	5
α-helix	17	1
β-strand	18-25	8	4
α-helix	29-31	3
β-strand	33-40	8	5
β-strand	44-51	8	5
β-strand	57-59	3	5
α-helix	63-65	3
β-strand	67-72	6	4
β-strand	77-82	6	4
α-helix	84-86	3
β-strand	88-95	8	5
β-strand	101-103	3	5
β-strand	107-111	5	5

Chain C: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
β-strand	5-7	3	6
β-strand	10-13	4	2
β-strand	19-24	6	6
β-strand	27C-27D	2	7
β-strand	30-31	2	7
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	6
β-strand	70-75	6	6
α-helix	80-82	3
β-strand	84-90	7	2
β-strand	98	1	2
β-strand	102-106	5	2

Chain D: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	8
β-strand	11-12	2	9
β-strand	18-25	8	8
β-strand	32-40	9	10
β-strand	44-51	8	10
β-strand	57-59	3	10
α-helix	61-63	3
β-strand	67-72	6	8
α-helix	73-75	3
β-strand	77-82	6	8
α-helix	84-86	3
β-strand	88-96	9	10
β-strand	101-103	3	10
β-strand	107-109	3	10
β-strand	110-111	2	9

Chain E: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	11
β-strand	10-13	4	12
α-helix	18	1
β-strand	19-25	7	11
β-strand	27C-27D	2	13
β-strand	30-31	2	13
β-strand	33-38	6	12
β-strand	45-49	5	12
β-strand	53-54	2	12
α-helix	55	1
β-strand	62-67	6	11
β-strand	70-75	6	11
β-strand	85-90	6	12
β-strand	98	1	12
β-strand	102-106	5	12

Chain F: 2 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	14
β-strand	11-12	2	15
β-strand	20-25	6	14
β-strand	33-40	8	16
β-strand	44-51	8	16
β-strand	57-59	3	16
α-helix	61-64	4
β-strand	69-72	4	14
β-strand	77-80	4	14
α-helix	84-86	3
β-strand	88-95	8	16
β-strand	101-103	3	16
β-strand	107-109	3	16
β-strand	110-111	2	15

Chain G: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	4-7	4	17
β-strand	10-13	4	18
β-strand	19-25	7	17
β-strand	27C-27D	2	19
β-strand	30-31	2	19
β-strand	33-38	6	18
β-strand	44-49	6	18
β-strand	53-54	2	18
α-helix	55	1
β-strand	62-67	6	17
β-strand	70-75	6	17
α-helix	80-82	3
β-strand	84-90	7	18
β-strand	98	1	18
β-strand	102-106	5	18

Chain H: 2 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	20
β-strand	11-12	2	21
β-strand	18-25	8	20
β-strand	33-39	7	22
β-strand	46-51	6	22
β-strand	57-59	3	22
α-helix	61-64	4
β-strand	67-72	6	20
β-strand	77-82	6	20
α-helix	84-86	3
β-strand	88-95	8	22
β-strand	101-103	3	22
β-strand	107-109	3	22
β-strand	110-111	2	21

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Protein (immunoglobulin (light chain))	A, C, E, G	protein	113	Mus musculus	Q9ERZ9
Protein (immunoglobulin (heavy chain))	B, D, F, H	protein	118	Mus musculus	P01820 (AlphaFold model)

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

>43C9_1 PROTEIN (IMMUNOGLOBULIN (LIGHT CHAIN)) (chains A, C, E, G)
DVVMTQTPSSLAMSVGQKVTMSCKSSQSLLNISNQKNYLAWYQQKPGQSPKLLVYFASTR
ESGVPDRFIGSGSGTDFTLTISSVQAEDQADYFCQQHYRAPRTFGGGTKLEIK

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

>43C9_2 PROTEIN (IMMUNOGLOBULIN (HEAVY CHAIN)) (chains B, D, F, H)
GQVQLVESGPGLVAPSQSLSITCTVSGISLSRYNVHWVRQSPGKGLEWLGMIWGGGSIEY
NPALKSRLSISKDNSKSQIFLKMNSLQTDDSAMYYCVSYGYGGDRFSYWGQGTLVTVS

Primary citation

Structural basis for amide hydrolysis catalyzed by the 43C9 antibody. Thayer, M.M., Olender, E.H., Arvai, A.S. et al. J Mol Biol (1999) 291:329-345. DOI 10.1006/jmbi.1999.2960 · PubMed

Other PDB entries of the same protein (UniProt Q9ERZ9), best resolution first:

43CA 2.3 Å, Crystallographic structure of the esterolytic and amidolytic 43C9 antibody with bound…

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