1GAF: 48G7 hybridoma line FAB

48G7 hybridoma line FAB complexed with hapten 5-(para-nitrophenyl phosphonate)-pentanoic acid. Determined by X-ray diffraction at 1.95 Å resolution. Released 11 Jul 1996.

Method: X-ray diffraction
Resolution: 1.95 Å
Organism: Homo sapiens
Chains: 2
Atoms: 3,453
Mol. weight: 47 kDa
Ligands: NPE
Released: 11 Jul 1996

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

Secondary structure: helices and β-sheets

1GAF contains 18 α-helices and 43 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: 10 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	3-6	4	6
β-strand	10-12	3	7
β-strand	18-25	8	6
α-helix	29-31	3
β-strand	34-39	6	7
β-strand	45-52	8	7
α-helix	53-55	3
β-strand	57-60	4	7
α-helix	62-64	3
β-strand	68-73	6	6
β-strand	78-83	6	6
α-helix	88-90	3
β-strand	92-97	6	7
α-helix	99-101	3
β-strand	104	1	7
β-strand	108-112	5	7
α-helix	115-117	3
β-strand	118	1	8
β-strand	121-125	5	9
β-strand	136-146	11	9
β-strand	147	1	8
β-strand	152-155	4	10
α-helix	156-158	3
β-strand	160	1	10
β-strand	164-166	3	9
α-helix	167-169	3
β-strand	170-171	2	9
β-strand	177-186	10	9
α-helix	187-189	3
β-strand	196-201	6	10
α-helix	202-204	3
β-strand	206-211	6	10

Chain L: 8 helices, 21 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	34-38	5	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	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	159-163	5	4
α-helix	164-167	4
β-strand	173-182	10	4
α-helix	183-186	4
β-strand	192-197	6	5
β-strand	205-208	4	5

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Chimeric 48G7 FAB	L	protein	214	Homo sapiens	P01834 (AlphaFold model)
Chimeric 48G7 FAB	H	protein	217	Homo sapiens	P01857 (AlphaFold model)

Sequence of entity 1 (L), FASTA

>1GAF_1 CHIMERIC 48G7 FAB (chains L)
DIQMTQSPSSLSASLGERVSLTCRASQEINGYLGWLQQKPDGTIKRLIYAASTLHSGVPK
RFSGSRSGSDYSLTISSLESEDFADYYCLQYASYPRTFGGGTKVEIKRTVAAPSVFIFPP
SDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNSQESVTEQDSKDSTYSLSSTLT
LSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC

Sequence of entity 2 (H), FASTA

>1GAF_2 CHIMERIC 48G7 FAB (chains H)
QVQLQQSGAELVKPGASVKLSCTASGFNIKDTYMHWVKQRPKQGLEWIGRIDPANVDTKY
DPKFQDKATITADTSSKTTYLQLSSLTSEDTAVYYCASYYGIYWGQGTTLTVSSASTKGP
SVFPLAPSSKSTSGGTAALGCLVKDYFPEPVTVSWNSGALTSGVHTFPAVLQSSGLYSLS
SVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSC

Ligands and cofactors

ID	Name	Formula	Copies
NPE	5-(para-nitrophenyl phosphonate)-pentanoic acid	C11 H13 N O7 P	1

Primary citation

The immunological evolution of catalysis. Patten, P.A., Gray, N.S., Yang, P.L. et al. Science (1996) 271:1086-1091. PubMed

Other PDB entries of the same protein (UniProt P01834 (AlphaFold model), which also has an AlphaFold model), best resolution first:

5EWI 1.6 Å, Crystal Structure of the Human Fab VRC38.01, an HIV-1 V1V2-Directed Neutralizing…
1NGZ 1.6 Å, Chimeric Germline Fab 7g12-apo
6N35 1.75 Å, Anti-HIV-1 Fab 2G12 + Man1-2 re-refinement
4XMP 1.78 Å, Crystal structure of broadly and potently neutralizing antibody VRC08 in complex with…
1N0X 1.8 Å, Crystal Structure of a Broadly Neutralizing Anti-HIV-1 Antibody in Complex with a…
3VH8 1.8 Å, KIR3DL1 in complex with HLA-B*5701
3X12 1.8 Å, Crystal structure of HLA-B*57:01.I80N
6B9Z 1.82 Å, Trastuzumab Fab v3
2VXQ 1.9 Å, Crystal structure of the major grass pollen allergen Phl p 2 in complex with its…
3D85 1.9 Å, Crystal structure of IL-23 in complex with neutralizing FAB
6BAH 1.9 Å, Trastuzumab Fab v3 with 5-diphenyl meditope variant
6DCV 1.9 Å, Crystal structure of human anti-tau antibody CBTAU-27.1

Browse structure collections

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