2CGR: IGG2B-kappa NC6.8 FAB

Local and transmitted conformational changes on complexation of an anti-sweetener FAB. Determined by X-ray diffraction at 2.2 Å resolution. Released 31 May 1994.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Mus musculus
Chains: 2
Atoms: 3,508
Mol. weight: 47.41 kDa
Ligands: GAS
Released: 31 May 1994

Explore 2CGR in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2CGR contains 9 α-helices and 42 β-strands across 2 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 H: 4 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	7
β-strand	10-12	3	8
β-strand	18-25	8	7
α-helix	29-31	3
β-strand	33-39	7	8
β-strand	45-52	8	8
β-strand	57-60	4	8
α-helix	62-64	3
β-strand	68-73	6	7
β-strand	78-83	6	7
α-helix	88-90	3
β-strand	92-99	8	8
β-strand	103-106	4	8
β-strand	110-114	5	8
α-helix	117-119	3
β-strand	120	1	9
β-strand	123-127	5	10
β-strand	138-148	11	10
β-strand	149	1	9
β-strand	154-158	5	11
β-strand	167-174	8	10
β-strand	177-187	11	10
β-strand	197-202	6	11
β-strand	207-212	6	11

Chain L: 5 helices, 22 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	30	1	3
β-strand	36	1	3
β-strand	38-43	6	2
β-strand	50-54	5	2
β-strand	58-59	2	2
β-strand	67-72	6	1
β-strand	75-80	6	1
α-helix	85-87	3
β-strand	89-95	7	2
α-helix	101	1
β-strand	102-103	2	2
β-strand	107-111	5	2
β-strand	116	1	4
β-strand	119-123	5	5
α-helix	124-126	3
α-helix	127-131	5
β-strand	134-144	11	5
β-strand	145	1	4
β-strand	150-155	6	6
β-strand	164-168	5	5
β-strand	178-187	10	5
α-helix	188-192	5
β-strand	196-202	7	6
β-strand	210-215	6	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
IGG2B-kappa NC6.8 FAB (light chain)	L	protein	219	Mus musculus	A2P1G9 (AlphaFold model)
IGG2B-kappa NC6.8 FAB (heavy chain)	H	protein	214	Mus musculus

Sequence of entity 1 (L), FASTA

>2CGR_1 IGG2B-KAPPA NC6.8 FAB (LIGHT CHAIN) (chains L)
ELVMTQSPLSLPVSLGDQASISCRPSQSLVHSNGNTYLHWYLQKPGQSPKLLIYRVSNRF
SGVPDRFSGSGSGTAFTLKISRVEAEDLGVYFCSQGTHVPYTFGGGTKLELKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM
SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRNEC

Sequence of entity 2 (H), FASTA

>2CGR_2 IGG2B-KAPPA NC6.8 FAB (HEAVY CHAIN) (chains H)
RVQLLESGAELMKPGASVQISCKATGYTFSEYWIEWVKERPGHGLEWIGEILPGSGRTNY
REKFKGKATFTADTSSNTAYMQLSSLTSEDSAVYYCTRGYSSMDYWGQGTSVTVSAAKTT
PPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFPALLQSGLYTM
SSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLE

Ligands and cofactors

ID	Name	Formula	Copies
GAS	N-(P-cyanophenyl)-N'-diphenylmethyl-guanidine-acetic acid	C23 H20 N4 O2	1

Primary citation

Local and transmitted conformational changes on complexation of an anti-sweetener Fab. Guddat, L.W., Shan, L., Anchin, J.M. et al. J Mol Biol (1994) 236:247-274. DOI 10.1006/jmbi.1994.1133 · PubMed

Other PDB entries of the same protein (UniProt A2P1G9 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1YNL 1.7 Å, Identification of Key residues of the NC6.8 Fab antibody fragment binding to synthetic…
1YNK 2.1 Å, Identification of Key residues of the NC6.8 Fab antibody fragment binding to synthetic…
1CGS 2.6 Å, Local and transmitted conformational changes on complexation of an anti-sweetener FAB
4ZXB 3.3 Å, Structure of the human insulin receptor ectodomain, IRDeltabeta construct, in complex…

Browse structure collections

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