4MS2: Ion transport protein

Structural basis of Ca2+ selectivity of a voltage-gated calcium channel. Determined by X-ray diffraction at 2.75 Å resolution. Released 27 Nov 2013.

Method: X-ray diffraction
Resolution: 2.75 Å
Organism: Arcobacter butzleri
Chains: 4
Atoms: 7,889
Mol. weight: 123.61 kDa
Ligands: CA, PX4
Released: 27 Nov 2013

Explore 4MS2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4MS2 contains 66 α-helices and 0 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: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	1002-1008	7
α-helix	1012-1031	20
α-helix	1035-1067	33
α-helix	1068-1073	6
α-helix	1075-1086	12
α-helix	1097-1101	5
α-helix	1102-1107	6
α-helix	1108-1111	4
α-helix	1116-1124	9
α-helix	1128-1130	3
α-helix	1131-1152	22
α-helix	1157-1160	4
α-helix	1163-1174	12
α-helix	1180-1184	5
α-helix	1185-1188	4
α-helix	1192-1194	3
α-helix	1195-1215	21

Chain B: 17 helices, 0 β-strands

Element	Residues	Length
α-helix	1002-1009	8
α-helix	1012-1031	20
α-helix	1035-1067	33
α-helix	1068-1073	6
α-helix	1075-1086	12
α-helix	1098-1101	4
α-helix	1102-1107	6
α-helix	1108-1112	5
α-helix	1116-1124	9
α-helix	1127-1152	26
α-helix	1157-1160	4
α-helix	1163-1174	12
α-helix	1179	1
α-helix	1180-1184	5
α-helix	1185-1188	4
α-helix	1192-1194	3
α-helix	1195-1215	21

Chain C: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	1002-1009	8
α-helix	1012-1031	20
α-helix	1035-1067	33
α-helix	1068-1070	3
α-helix	1075-1086	12
α-helix	1097-1101	5
α-helix	1102-1107	6
α-helix	1108-1111	4
α-helix	1114-1124	11
α-helix	1128-1130	3
α-helix	1131-1152	22
α-helix	1157-1160	4
α-helix	1163-1174	12
α-helix	1180-1184	5
α-helix	1185-1190	6
α-helix	1195-1216	22

Chain D: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	1002-1009	8
α-helix	1012-1031	20
α-helix	1035-1065	31
α-helix	1068-1073	6
α-helix	1075-1086	12
α-helix	1097-1101	5
α-helix	1102-1107	6
α-helix	1108-1112	5
α-helix	1116-1124	9
α-helix	1128-1130	3
α-helix	1131-1152	22
α-helix	1157-1160	4
α-helix	1163-1174	12
α-helix	1180-1184	5
α-helix	1185-1190	6
α-helix	1194-1218	25

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Ion transport protein	A, B, C, D	protein	237	Arcobacter butzleri	A8EVM5 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4MS2_1 Ion transport protein (chains A, B, C, D)
MDYKDDDDKGSLVPRGSHMYLRITNIVESSFFTKFIIYLIVLNGITMGLETSKTFMQSFG
VYTTLFNQIVITIFTIEIILRIYVHRISFFKDPWSLFDFFVVAISLVPTSSGFEILRVLR
VLRLFRLVTAVPQMRKIVSALISVIPGMLSVIALMTLFFYIFAIMATQLFGERFPEWFGT
LGESFYTLFQVMTLDDWSNGIVRPLMEVYPYAWVFFIPFIFVVTFVMINLVVAICVD

Ligands and cofactors

ID	Name	Formula	Copies
CA	Calcium ion	Ca	5
PX4	1,2-dimyristoyl-sn-glycero-3-phosphocholine	C36 H73 N O8 P	20

Primary citation

Structural basis for Ca2+ selectivity of a voltage-gated calcium channel. Tang, L., Gamal El-Din, T.M., Payandeh, J. et al. Nature (2014) 505:56-61. DOI 10.1038/nature12775 · PubMed

Other PDB entries of the same protein (UniProt A8EVM5 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6MWD 2.33 Å, NavAb Voltage-gated Sodium Channel, residues 1-239 with mutation T206S
6MWA 2.4 Å, NavAb Voltage-gated Sodium Channel, residues 1-239
9UC1 2.5 Å, Crystal structure of voltage-gated sodium channel NavAb N49K/S178T mutant
6MWG 2.5 Å, NavAb Voltage-gated Sodium Channel, residues 1-239, with mutation T206V
6C1M 2.52 Å, NavAb NormoPP mutant
8DIV 2.54 Å, Crystal structure of NavAb I22V as a basis for the human Nav1.7 Inherited…
6MWB 2.6 Å, NavAb Voltage-gated Sodium Channel, residues 1-239 with mutation T206A
8VGL 2.6 Å, CryoEM structure of Nav1.7 in complex with wild type Fab 7A9
8VGM 2.6 Å, CryoEM structure of Nav1.7 in complex with engineered conformationally rigid Fab 7A9.4DS
3RVY 2.7 Å, Crystal structure of the NavAb voltage-gated sodium channel (Ile217Cys, 2.7 A)
5KLB 2.7 Å, Crystal structure of the CavAb voltage-gated calcium channel(wild-type, 2.7A)
6C1K 2.7 Å, HypoPP mutant with ligand1

Browse structure collections

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