1ETZ: FAB NC10.14 - light chain

The three-dimensional structure of an anti-sweetener FAB, NC10.14, shows the extent of structural diversity in antigen recognition by immunoglobulins. Determined by X-ray diffraction at 2.6 Å resolution. Released 18 Oct 2000.

Method: X-ray diffraction
Resolution: 2.6 Å
Organism: Mus musculus
Chains: 4
Atoms: 6,833
Mol. weight: 96.04 kDa
Ligands: GAS
Released: 18 Oct 2000

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

Secondary structure: helices and β-sheets

1ETZ contains 24 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, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	13
β-strand	9-12	4	14
β-strand	17-22	6	15
β-strand	23-24	2	13
β-strand	27	1	13
α-helix	31-33	3
β-strand	36-41	6	14
β-strand	45-51	7	14
β-strand	55-56	2	14
β-strand	64-69	6	15
β-strand	72-78	7	15
α-helix	82-84	3
β-strand	86-93	8	14
β-strand	98-100	3	14
β-strand	104-108	5	14
β-strand	114	1	16
β-strand	119-121	3	17
α-helix	122-124	3
α-helix	125-128	4
β-strand	132-142	11	17
β-strand	143	1	16
β-strand	148-153	6	18
β-strand	156-157	2	18
α-helix	158	1
β-strand	162-164	3	17
β-strand	168-169	2	17
β-strand	175-184	10	17
α-helix	185-189	5
β-strand	193-200	8	18
β-strand	203-210	8	18

Chain B: 5 helices, 20 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	19
β-strand	11-12	2	20
α-helix	16-17	2
β-strand	18-25	8	19
β-strand	34-42	9	21
β-strand	48-54	7	21
β-strand	59-61	3	21
β-strand	69-74	6	19
β-strand	79-84	6	19
α-helix	89-91	3
β-strand	93-105	13	21
β-strand	108-116	9	21
β-strand	120-122	3	21
β-strand	123-124	2	20
α-helix	130-132	3
β-strand	133-137	5	22
β-strand	148-158	11	22
β-strand	164-166	3	23
β-strand	175-178	4	22
α-helix	179-181	3
β-strand	182-184	3	22
β-strand	187-197	11	22
α-helix	198-200	3
β-strand	207-212	6	23
β-strand	217-222	6	23

Chain H: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	7
β-strand	11-12	2	8
α-helix	16-17	2
β-strand	18-25	8	7
β-strand	34-42	9	9
β-strand	48-54	7	9
β-strand	59-61	3	9
α-helix	66-68	3
β-strand	69-74	6	7
β-strand	79-84	6	7
α-helix	89-91	3
β-strand	93-105	13	9
β-strand	108-116	9	9
β-strand	120-122	3	9
β-strand	123-124	2	8
α-helix	127-129	3
β-strand	130	1	10
α-helix	131-132	2
β-strand	133-137	5	11
β-strand	148-156	9	11
β-strand	159	1	10
β-strand	164-168	5	12
β-strand	177-178	2	11
α-helix	179-181	3
β-strand	189-197	9	11
β-strand	207-212	6	12
β-strand	217-222	6	12

Chain L: 7 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	1
β-strand	9-12	4	2
β-strand	17-22	6	3
β-strand	23-24	2	1
β-strand	27	1	1
α-helix	31-33	3
β-strand	36-41	6	2
β-strand	45-51	7	2
β-strand	55-56	2	2
α-helix	57	1
β-strand	64-69	6	3
β-strand	72-78	7	3
α-helix	82-84	3
β-strand	86-93	8	2
β-strand	98-100	3	2
β-strand	104-108	5	2
β-strand	114	1	4
β-strand	117-121	5	5
α-helix	122-124	3
α-helix	125-128	4
β-strand	132-142	11	5
β-strand	143	1	4
β-strand	148-153	6	6
β-strand	156-157	2	6
β-strand	162-164	3	5
α-helix	165-167	3
β-strand	168-169	2	5
β-strand	175-184	10	5
α-helix	185-189	5
β-strand	193-200	8	6
β-strand	203-210	8	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
FAB NC10.14 - light chain	A, L	protein	215	Mus musculus	G0YP42 (AlphaFold model)
FAB NC10.14 - heavy chain	B, H	protein	228	Mus musculus	P01867 (AlphaFold model)

Sequence of entity 1 (A, L), FASTA

>1ETZ_1 FAB NC10.14 - LIGHT CHAIN (chains A, L)
FAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYAIWVQEKPDHLFSGLIGGTNNRVPGV
PARFSGSLIGDKAALTVTGAQTEDEAIYFCALWYSNHWVFGGGTKLTVLGQPKSSPSVTL
FTPSSEELETNKATLVCTITDFYPGVVTVDWKVDGTPVTQGMETTQPSKQSNNKYMASSY
LTLTARAWERHSSYSCQVTHEGHTVEKSLSRAECS

Sequence of entity 2 (B, H), FASTA

>1ETZ_2 FAB NC10.14 - HEAVY CHAIN (chains B, H)
QVTLKESGPGILQPSQTLSLTCSFSGFSLSTSGMGVGWIRQPSGEGLEWLADIWWNDKKY
YNPSLKSRLTVSKDTSSNQVFLKITSVDTSDTATYHCARRTFSYYYGSSFYYFDNWGQGT
TLTVSSAKTTPPSVYPLAPGCGDTTGSSVTLGCLVKGYFPESVTVTWNSGSLSSSVHTFP
ALLQSGLYTMSSSVTVPSSTWPSQTVTCSVAHPASSTTVDKKLEPSGP

Ligands and cofactors

ID	Name	Formula	Copies
GAS	N-(P-cyanophenyl)-N'-diphenylmethyl-guanidine-acetic acid	C23 H20 N4 O2	2

Primary citation

The three-dimensional structure of a complex of a murine Fab (NC10. 14) with a potent sweetener (NC174): an illustration of structural diversity in antigen recognition by immunoglobulins. Guddat, L.W., Shan, L., Broomell, C. et al. J Mol Biol (2000) 302:853-872. DOI 10.1006/jmbi.2000.4083 · PubMed

Other PDB entries of the same protein (UniProt G0YP42 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1NGP 2.4 Å, N1G9 (IgG1-lambda) FAB fragment complexed with (4-hydroxy-3-nitrophenyl) acetate
1NGQ 2.4 Å, N1G9 (IgG1-lambda) FAB fragment
1PG7 2.5 Å, Murine 6A6 Fab in complex with humanized anti-Tissue Factor D3H44 Fab
2OP4 2.85 Å, Crystal Structure of Quorum-Quenching Antibody 1G9
2NTF 3.18 Å, Crystal Structure of a Quorum-Quenching Antibody in Complex with an N-Acyl-L-Homoserine…
2VIR 3.25 Å, Influenza virus hemagglutinin complexed with a neutralizing antibody
2VIS 3.25 Å, Influenza virus hemagglutinin, (ESCAPE) mutant with thr 131 replaced by ile, complexed…
2VIT 3.25 Å, Influenza virus hemagglutinin, mutant with thr 155 replaced by ile, complexed with a…
3RHW 3.26 Å, C. elegans glutamate-gated chloride channel (GluCl) in complex with Fab and ivermectin
3RIF 3.35 Å, C. elegans glutamate-gated chloride channel (GluCl) in complex with Fab, ivermectin and…
3RI5 3.4 Å, C. elegans glutamate-gated chloride channel (GluCl) in complex with Fab, ivermectin and…
3RIA 3.8 Å, C. elegans glutamate-gated chloride channel (GluCl) in complex with Fab, ivermectin and…

Browse structure collections

About this viewer

MolViewer shows 1ETZ directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.