43CA: Protein)

Crystallographic structure of the esterolytic and amidolytic 43C9 antibody with bound P-nitrophenol. Determined by X-ray diffraction at 2.3 Å resolution. Released 18 Aug 1999.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Mus musculus
Chains: 8
Atoms: 7,271
Mol. weight: 101.45 kDa
Ligands: NPO
Released: 18 Aug 1999

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

Secondary structure: helices and β-sheets

43CA contains 16 α-helices and 100 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	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	102-106	5	2

Chain B: 1 helix, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	4
β-strand	11-12	2	5
β-strand	18-25	8	4
β-strand	32-40	9	6
β-strand	44-51	8	6
β-strand	57-59	3	6
β-strand	67-72	6	4
β-strand	77-82	6	4
α-helix	84-86	3
β-strand	88-96	9	6
β-strand	101-103	3	6
β-strand	107-109	3	6
β-strand	110-111	2	5

Chain C: 3 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	7
β-strand	10-13	4	2
α-helix	17-18	2
β-strand	19-25	7	7
β-strand	27C-27D	2	8
β-strand	30-31	2	8
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	7
β-strand	70-75	6	7
α-helix	80-82	3
β-strand	84-90	7	2
β-strand	98	1	2
β-strand	102-106	5	2

Chain D: 2 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	9
β-strand	11-12	2	10
β-strand	18-25	8	9
β-strand	32-40	9	11
β-strand	44-51	8	11
β-strand	57-59	3	11
α-helix	61-64	4
β-strand	67-72	6	9
β-strand	77-82	6	9
α-helix	84-86	3
β-strand	88-96	9	11
β-strand	101-103	3	11
β-strand	107-109	3	11
β-strand	110-111	2	10

Chain E: 1 helix, 13 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
β-strand	4-7	4	12
β-strand	10-13	4	13
β-strand	19-25	7	12
β-strand	27C-27D	2	14
β-strand	30-31	2	14
β-strand	33-38	6	13
β-strand	45-49	5	13
β-strand	53-54	2	13
β-strand	62-67	6	12
β-strand	70-75	6	12
β-strand	84-90	7	13
β-strand	98	1	13
β-strand	102-106	5	13

Chain F: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	15
β-strand	11-12	2	16
α-helix	16-17	2
β-strand	18-25	8	15
β-strand	32-40	9	17
β-strand	44-51	8	17
β-strand	57-59	3	17
α-helix	61-66	6
β-strand	67-72	6	15
β-strand	77-82	6	15
α-helix	84-86	3
β-strand	88-96	9	17
β-strand	101-103	3	17
β-strand	107-109	3	17
β-strand	110-111	2	16

Chain G: 2 helices, 13 β-strands

Element	Residues	Length	Sheet
β-strand	5-7	3	18
β-strand	10-13	4	19
β-strand	19-24	6	18
β-strand	27C-27D	2	20
β-strand	30-31	2	20
β-strand	33-38	6	19
β-strand	45-49	5	19
β-strand	53-54	2	19
α-helix	55	1
β-strand	62-67	6	18
β-strand	70-75	6	18
α-helix	80-82	3
β-strand	84-90	7	19
β-strand	98	1	19
β-strand	102-106	5	19

Chain H: 2 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	21
β-strand	11-12	2	22
β-strand	18-25	8	21
β-strand	33-40	8	23
β-strand	44-51	8	23
β-strand	57-59	3	23
α-helix	61-64	4
β-strand	67-72	6	21
β-strand	77-82	6	21
α-helix	84-86	3
β-strand	88-95	8	23
β-strand	101-103	3	23
β-strand	107-109	3	23
β-strand	110-111	2	22

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	117	Mus musculus	P01820 (AlphaFold model)

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

>43CA_1 PROTEIN (IMMUNOGLOBULIN (LIGHT CHAIN)) (chains A, C, E, G)
DVVMTQTPSSLAMSVGQKVTMSCKSSQSLLNISNQKNYLAWYQQKPGQSPKLLVYFASTR
ESGVPDRFIGSGSGTDFTLTISSVQAEDQADYFCQQHYRAPRTFGGGTKLEIK

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

>43CA_2 PROTEIN (IMMUNOGLOBULIN (HEAVY CHAIN)) (chains B, D, F, H)
QVQLVESGPGLVAPSQSLSITCTVSGISLSRYNVHWVRQSPGKGLEWLGMIWGGGSIEYN
PALKSRLSISKDNSKSQIFLKMNSLQTDDSAMYYCVSYGYGGDRFSYWGQGTLVTVS

Ligands and cofactors

ID	Name	Formula	Copies
NPO	P-nitrophenol	C6 H5 N O3	4

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:

43C9 2.2 Å, Crystallographic structure of the esterolytic and amidolytic 43C9 antibody

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