2H8P: FAB heavy chain

Structure of a K channel with an amide to ester substitution in the selectivity filter. Determined by X-ray diffraction at 2.25 Å resolution. Released 12 Sept 2006.

Method: X-ray diffraction
Resolution: 2.25 Å
Organisms: Mus musculus, synthetic construct
Chains: 3
Atoms: 4,177
Mol. weight: 58.17 kDa
Ligands: B3H
Released: 12 Sept 2006

Explore 2H8P in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2H8P contains 16 α-helices and 43 β-strands across 3 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: 5 helices, 22 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	1
β-strand	9-12	4	2
β-strand	18-24	7	1
β-strand	33-39	7	2
β-strand	45-52	8	2
β-strand	57-60	4	2
β-strand	68-73	6	1
β-strand	78-83	6	1
α-helix	88-90	3
β-strand	92-99	8	2
β-strand	107-108	2	2
β-strand	112-116	5	2
β-strand	122	1	3
α-helix	123-124	2
β-strand	125-129	5	4
β-strand	140-150	11	4
β-strand	151	1	3
β-strand	156-159	4	5
β-strand	164	1	5
β-strand	168-170	3	4
α-helix	171-173	3
β-strand	174-175	2	4
β-strand	180-189	10	4
α-helix	190-192	3
β-strand	199-204	6	5
α-helix	205-207	3
β-strand	209-214	6	5

Chain B: 8 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-6	3	6
β-strand	10-13	4	7
β-strand	19-25	7	6
β-strand	33-38	6	7
α-helix	42-44	3
β-strand	45-49	5	7
β-strand	53-54	2	7
β-strand	62-67	6	6
β-strand	70-75	6	6
α-helix	80-82	3
β-strand	85-90	6	7
α-helix	96	1
β-strand	97-98	2	7
β-strand	102-106	5	7
β-strand	111	1	8
β-strand	114-118	5	9
α-helix	119-121	3
α-helix	122-125	4
β-strand	130-139	10	9
β-strand	140	1	8
β-strand	145-150	6	10
β-strand	153-155	3	10
β-strand	159-163	5	9
α-helix	164-167	4
β-strand	173-181	9	9
α-helix	183-187	5
β-strand	191-197	7	10
α-helix	204	1
β-strand	205-210	6	10

Chain C: 3 helices, 0 β-strands

Element	Residues	Length
α-helix	24-51	28
α-helix	62-73	12
α-helix	86-118	33

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
FAB heavy chain	A	protein	219	Mus musculus	Q569B4 (AlphaFold model)
FAB light chain	B	protein	212	Mus musculus	P01837 (AlphaFold model)
KcsA Channel	C	protein	101	synthetic construct	P0A334 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2H8P_1 FAB heavy chain (chains A)
QVQLQQPGAELVKPGASVKLSCKASGYTFTSDWIHWVKQRPGHGLEWIGEIIPSYGRANY
NEKIQKKATLTADKSSSTAFMQLSSLTSEDSAVYYCARERGDGYFAVWGAGTTVTVSSAK
TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRD

Sequence of entity 2 (B), FASTA

>2H8P_2 FAB light chain (chains B)
DILLTQSPAILSVSPGERVSFSCRASQSIGTDIHWYQQRTNGSPRLLIKYASESISGIPS
RFSGSGSGTDFTLSINSVESEDIANYYCQQSNRWPFTFGSGTKLEIKRADAAPTVSIFPP
SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT
LTKDEYERHNSYTCEATHKTSTSPIVKSFNRN

Sequence of entity 3 (C), FASTA

>2H8P_3 KcsA Channel (chains C)
SALHWRAAGAATVLLVIVLLAGSYLAVLAERGAPGAQLITYPRALWWACETATTVGYXDL
YPVTLWGRLVAVVVMVAGITSFGLVTAALATWFVGREQERR

Ligands and cofactors

ID	Name	Formula	Copies
B3H	(2S)-2-(butyryloxy)-3-hydroxypropyl nonanoate	C16 H30 O5	1

Water and common crystallization additives (K) are not listed.

Primary citation

Structural and Functional Consequences of an Amide-to-Ester Substitution in the Selectivity Filter of a Potassium Channel. Valiyaveetil, F.I., Sekedat, M., Mackinnon, R. et al. J Am Chem Soc (2006) 128:11591-11599. DOI 10.1021/ja0631955 · PubMed

Other PDB entries of the same protein (UniProt Q569B4 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2J4W 2.5 Å, Structure of a Plasmodium vivax apical membrane antigen 1-Fab F8.12.19 complex
2HG5 2.75 Å, Cs+ complex of a K channel with an amide to ester substitution in the selectivity filter

Browse structure collections

About this viewer

MolViewer shows 2H8P 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.