4MSW: Y78 ester mutant of KcsA in high K+

Y78 ester mutant of KcsA in high K+. Determined by X-ray diffraction at 2.06 Å resolution. Released 30 Oct 2013.

Method: X-ray diffraction
Resolution: 2.06 Å
Organisms: Mus musculus, Streptomyces lividans
Chains: 3
Atoms: 4,353
Mol. weight: 58.7 kDa
Ligands: DGA
Released: 30 Oct 2013

Explore 4MSW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4MSW 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: 7 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	46-52	7	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
α-helix	120-121	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
α-helix	160-162	3
β-strand	164	1	5
β-strand	168-170	3	4
α-helix	171-173	3
β-strand	174-176	3	4
β-strand	179-189	11	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: 6 helices, 21 β-strands

Element	Residues	Length	Sheet
β-strand	4-5	2	6
β-strand	10-13	4	7
β-strand	19-25	7	6
β-strand	33-38	6	7
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	122-126	5
β-strand	129-139	11	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	173-182	10	9
α-helix	183-187	5
β-strand	191-197	7	10
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	85-120	36

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Antibody FAB fragment heavy chain	A	protein	219	Mus musculus
Monoclonal 11D8 anti-human butyrylcholinesterase (BChE) light chain	B	protein	212	Mus musculus	A0A0M4KEQ7 (AlphaFold model)
pH-gated potassium channel KcsA	C	protein	102	Streptomyces lividans	P0A334 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4MSW_1 ANTIBODY FAB FRAGMENT HEAVY CHAIN (chains A)
QVQLQQPGAELVKPGASVKLSCKASGYTFTSDWIHWVKQRPGHGLEWIGEIIPSYGRANY
NEKIQKKATLTADKSSSTAFMQLSSLTSEDSAVYYCARERGDGYFAVWGAGTTVTVSSAK
TTPPSVYPLAPGSAAQTNSMVTLGCLVKGYFPEPVTVTWNSGSLSSGVHTFPAVLQSDLY
TLSSSVTVPSSSWPSETVTCNVAHPASSTKVDKKIVPRD

Sequence of entity 2 (B), FASTA

>4MSW_2 Monoclonal 11D8 anti-human butyrylcholinesterase (BChE) light chain (chains B)
DILLTQSPAILSVSPGERVSFSCRASQSIGTDIHWYQQRTNGSPRLLIKYASESISGIPS
RFSGSGSGTDFTLSINSVESEDIANYYCQQSNRWPFTFGSGTKLEIKRADAAPTVSIFPP
SSEQLTSGGASVVCFLNNFYPKDINVKWKIDGSERQNGVLNSWTDQDSKDSTYSMSSTLT
LTKDEYERHNSYTCEATHKTSTSPIVKSFNRN

Sequence of entity 3 (C), FASTA

>4MSW_3 pH-gated potassium channel KcsA (chains C)
SALHWRAAGAATVLLVIVLLAGSYLAVLAERGAPGAQLITYPRALWWSVETATTVYGDLY
PVTLWGRLVAVVVMVAGITSFGLVTAALATWFVGREQERRGH

Ligands and cofactors

ID	Name	Formula	Copies
DGA	Diacyl glycerol	C39 H76 O5	1

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

Primary citation

Using protein backbone mutagenesis to dissect the link between ion occupancy and C-type inactivation in K+ channels. Matulef, K., Komarov, A.G., Costantino, C.A. et al. Proc Natl Acad Sci U S A (2013) 110:17886-17891. DOI 10.1073/pnas.1314356110 · PubMed

Other PDB entries of the same protein (UniProt A0A0M4KEQ7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2OZ4 2.7 Å, Structural Plasticity in IgSF Domain 4 of ICAM-1 Mediates Cell Surface Dimerization

Browse structure collections

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