2G5B: 6A7 Fab Light Chain

Crystal Structure of the anti-Bax monoclonal antibody 6A7 and a Bax peptide. Determined by X-ray diffraction at 2.3 Å resolution. Released 25 Jul 2006.

Method: X-ray diffraction
Resolution: 2.3 Å
Organism: Mus musculus
Chains: 12
Atoms: 14,198
Mol. weight: 197.96 kDa
Released: 25 Jul 2006

Explore 2G5B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2G5B contains 64 α-helices and 185 β-strands across 12 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: 7 helices, 23 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	30-30A	2	3
β-strand	30F-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	96-97	2	2
β-strand	101-105	5	2
α-helix	106	1
β-strand	110	1	4
β-strand	113-117	5	5
α-helix	118-120	3
α-helix	121-125	5
β-strand	128-138	11	5
β-strand	139	1	4
β-strand	144-149	6	6
β-strand	152-154	3	6
β-strand	158-162	5	5
β-strand	172-181	10	5
α-helix	182-186	5
β-strand	190-196	7	6
α-helix	203	1
β-strand	204-209	6	6

Chain B: 8 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	7
β-strand	11-12	2	8
β-strand	18-25	8	7
α-helix	29-31	3
β-strand	33-39	7	9
β-strand	46-51	6	9
α-helix	52B-52D	3
β-strand	55-57	3	9
β-strand	65-70	6	7
β-strand	75-80	6	7
α-helix	84-86	3
β-strand	88-96	9	9
α-helix	98-100A	3
β-strand	100D-101	5	9
β-strand	105-107	3	9
β-strand	108-109	2	8
β-strand	115	1	10
β-strand	118-122	5	11
β-strand	133-143	11	11
β-strand	144	1	10
β-strand	149-152	4	12
α-helix	153-155	3
β-strand	157	1	12
β-strand	161-163	3	11
α-helix	164-166	3
β-strand	167-168	2	11
β-strand	173-182	10	11
α-helix	183-185	3
β-strand	192-197	6	12
α-helix	198-200	3
β-strand	202-207	6	12

Chains C, E and G: 6 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	4-7	4	13
β-strand	10-13	4	14
β-strand	19-25	7	13
β-strand	30-30A	2	15
β-strand	30F-31	2	15
β-strand	33-38	6	14
β-strand	45-49	5	14
β-strand	53-54	2	14
α-helix	55	1
β-strand	62-67	6	13
β-strand	70-75	6	13
α-helix	80-82	3
β-strand	84-90	7	14
β-strand	96-97	2	14
β-strand	101-105	5	14
β-strand	110	1	16
β-strand	113-117	5	17
α-helix	118-120	3
α-helix	121-125	5
β-strand	128-138	11	17
β-strand	139	1	16
β-strand	144-149	6	18
β-strand	152-154	3	18
β-strand	158-162	5	17
β-strand	172-181	10	17
α-helix	182-186	5
β-strand	190-196	7	18
α-helix	203	1
β-strand	204-209	6	18

Chain D: 8 helices, 24 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	19
β-strand	11-12	2	20
β-strand	18-25	8	19
α-helix	29-31	3
β-strand	33-39	7	21
β-strand	46-51	6	21
α-helix	52B-52D	3
β-strand	55-57	3	21
β-strand	62	1	19
β-strand	65-70	6	19
β-strand	75-80	6	19
α-helix	84-86	3
β-strand	88-96	9	21
α-helix	98-100A	3
β-strand	100D-101	5	21
β-strand	105-107	3	21
β-strand	108-109	2	20
β-strand	115	1	22
β-strand	118-122	5	23
β-strand	133-143	11	23
β-strand	144	1	22
β-strand	149-152	4	24
α-helix	153-155	3
β-strand	157	1	24
β-strand	161-163	3	23
α-helix	164-166	3
β-strand	167-168	2	23
β-strand	173-182	10	23
α-helix	183-185	3
β-strand	192-197	6	24
α-helix	198-200	3
β-strand	202-207	6	24

Chain F: 10 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	31
β-strand	11-12	2	32
β-strand	18-25	8	31
α-helix	29-31	3
β-strand	33-39	7	33
β-strand	46-51	6	33
α-helix	52B-52D	3
β-strand	55-57	3	33
α-helix	59-61	3
β-strand	65-70	6	31
β-strand	75-80	6	31
α-helix	84-86	3
β-strand	88-96	9	33
α-helix	98-100A	3
β-strand	100D-101	5	33
β-strand	105-107	3	33
β-strand	108-109	2	32
α-helix	113-114	2
β-strand	115	1	34
α-helix	116-117	2
β-strand	118-122	5	35
β-strand	133-143	11	35
β-strand	144	1	34
β-strand	149-152	4	36
β-strand	157	1	36
β-strand	161-163	3	35
α-helix	164-166	3
β-strand	167-168	2	35
β-strand	173-182	10	35
α-helix	183-185	3
β-strand	192-197	6	36
α-helix	198-200	3
β-strand	202-207	6	36

Chain H: 9 helices, 23 β-strands

Element	Residues	Length	Sheet
β-strand	3-7	5	43
β-strand	11-12	2	44
β-strand	18-25	8	43
α-helix	29-31	3
β-strand	33-39	7	45
β-strand	46-51	6	45
α-helix	52B-52D	3
β-strand	55-57	3	45
β-strand	65-70	6	43
β-strand	75-80	6	43
α-helix	84-86	3
β-strand	88-96	9	45
α-helix	98-100A	3
β-strand	100D-101	5	45
β-strand	105-107	3	45
β-strand	108-109	2	44
β-strand	115	1	46
α-helix	116-117	2
β-strand	118-122	5	47
β-strand	133-143	11	47
β-strand	144	1	46
β-strand	149-152	4	48
α-helix	153-155	3
β-strand	157	1	48
β-strand	161-163	3	47
α-helix	164-166	3
β-strand	167-168	2	47
β-strand	173-182	10	47
α-helix	183-185	3
β-strand	192-197	6	48
α-helix	198-200	3
β-strand	202-207	6	48

Chains I, J, K and L: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	602-604	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
6A7 Fab Light Chain	A, C, E, G	protein	217	Mus musculus	P01837 (AlphaFold model)
6A7 Fab Heavy Chain	B, D, F, H	protein	222	Mus musculus	P84751 (AlphaFold model)
Bax Peptide	I, J, K, L	protein	7		Q07812 (AlphaFold model)

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

>2G5B_1 6A7 Fab Light Chain (chains A, C, E, G)
DIVMSQSPSSLAVSAGERVTMTCKSSQSLFNSKTRRNYLAWYQQKPGQSPKLLIYWASTR
ESGVPDRFTGSGSGTEFTLTISSVQAEDLAVYYCKQSYNLRTFGGGTKLEIKRADAAPTV
SIFPPSSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSM
SSTLTLTKDEYERHNSYTCEATHKTSTSPIVKSFNRN

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

>2G5B_2 6A7 Fab Heavy Chain (chains B, D, F, H)
EVNLVESGGGLVQPGGSLRLSCATSGFTFIDNYMSWVRQPPGKALEWLGFIRNKVNGYTT
EYGPSVKGRFTISRDDSQSILYLQMNTLRTEDSATYYCVRDNGSDYRWYFDVWGAGTTVT
VSSAKTTPPSVYPLAPGSAAGTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVL
QSDLYTLSSSVTVPSSTWPSETVTCNVAHPASSTKVDKKIVP

Sequence of entity 3 (I, J, K, L), FASTA

>2G5B_3 Bax Peptide (chains I, J, K, L)
PTSSEQI

Primary citation

Elucidation of some Bax conformational changes through crystallization of an antibody-peptide complex. Peyerl, F.W., Dai, S., Murphy, G.A. et al. Cell Death Differ (2007) 14:447-452. DOI 10.1038/sj.cdd.4402025 · PubMed

Other PDB entries of the same protein (UniProt P01837 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3D9A 1.2 Å, High Resolution Crystal Structure Structure of HyHel10 Fab Complexed to Hen Egg Lysozyme
1RUR 1.5 Å, Crystal Structure (I) of native Diels-Alder antibody 13G5 Fab at pH 8.0 with a data set…
2AJU 1.5 Å, Cyrstal structure of cocaine catalytic antibody 7A1 Fab'
2AJV 1.5 Å, Crystal Structure of Cocaine catalytic Antibody 7A1 Fab' in Complex with Cocaine
2W60 1.5 Å, Anti citrullinated Collagen type 2 antibody acc4
2W9D 1.57 Å, Structure of Fab fragment of the ICSM 18 - anti-Prp therapeutic antibody at 1.57 A…
3BKJ 1.59 Å, Crystal structure of Fab wo2 bound to the n terminal domain of amyloid beta peptide (1-16)
3BAE 1.59 Å, Crystal structure of Fab WO2 bound to the N terminal domain of Amyloid beta peptide (1-28)
2R1Y 1.6 Å, Crystal structure of S25-2 Fab in complex with Kdo analogues
2R2B 1.6 Å, Crystal structure of S25-2 Fab in complex with Kdo analogues
3BKM 1.6 Å, Structure of anti-amyloid-beta Fab WO2 (Form A, P212121)
3CFB 1.6 Å, High-resolution structure of blue fluorescent antibody EP2-19G2 in complex with stilbene…

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