Structure of CavAb in complex with Diltiazem and Amlodipine. Determined by X-ray diffraction at 2.8 Å resolution. Released 23 Oct 2019.
Explore 6KE5 in 3D Show helices and sheets RCSB PDB PDBe
6KE5 contains 69 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1004-1007 | 4 | |
| α-helix | 1014-1032 | 19 | |
| α-helix | 1037-1040 | 4 | |
| α-helix | 1042-1064 | 23 | |
| α-helix | 1075-1087 | 13 | |
| α-helix | 1101-1107 | 7 | |
| α-helix | 1108-1111 | 4 | |
| α-helix | 1115-1123 | 9 | |
| α-helix | 1124-1126 | 3 | |
| α-helix | 1131-1151 | 21 | |
| α-helix | 1157-1160 | 4 | |
| α-helix | 1163-1175 | 13 | |
| α-helix | 1179 | 1 | |
| α-helix | 1180-1184 | 5 | |
| α-helix | 1185-1190 | 6 | |
| α-helix | 1199-1217 | 19 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1003-1009 | 7 | |
| α-helix | 1013-1033 | 21 | |
| α-helix | 1035-1038 | 4 | |
| α-helix | 1042-1067 | 26 | |
| α-helix | 1068-1073 | 6 | |
| α-helix | 1075-1086 | 12 | |
| α-helix | 1096-1101 | 6 | |
| α-helix | 1102-1105 | 4 | |
| α-helix | 1107-1112 | 6 | |
| α-helix | 1116-1124 | 9 | |
| α-helix | 1127-1151 | 25 | |
| 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 | 1195-1210 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1006-1009 | 4 | |
| α-helix | 1012-1030 | 19 | |
| α-helix | 1037-1040 | 4 | |
| α-helix | 1042-1044 | 3 | |
| α-helix | 1048-1066 | 19 | |
| α-helix | 1071-1073 | 3 | |
| α-helix | 1075-1087 | 13 | |
| α-helix | 1102-1109 | 8 | |
| α-helix | 1114-1123 | 10 | |
| α-helix | 1127-1138 | 12 | |
| α-helix | 1140-1149 | 10 | |
| α-helix | 1157-1160 | 4 | |
| α-helix | 1163-1174 | 12 | |
| α-helix | 1180-1184 | 5 | |
| α-helix | 1185-1187 | 3 | |
| α-helix | 1194-1214 | 21 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1002-1008 | 7 | |
| α-helix | 1012-1014 | 3 | |
| α-helix | 1015-1019 | 5 | |
| α-helix | 1020-1026 | 7 | |
| α-helix | 1028-1031 | 4 | |
| α-helix | 1036-1041 | 6 | |
| α-helix | 1043-1066 | 24 | |
| α-helix | 1075-1085 | 11 | |
| α-helix | 1101-1107 | 7 | |
| α-helix | 1108-1111 | 4 | |
| α-helix | 1114-1124 | 11 | |
| α-helix | 1134-1152 | 19 | |
| α-helix | 1163-1174 | 12 | |
| α-helix | 1180-1184 | 5 | |
| α-helix | 1185-1190 | 6 | |
| α-helix | 1192-1194 | 3 | |
| α-helix | 1195-1210 | 16 | |
| α-helix | 1214-1221 | 8 | |
| α-helix | 1224-1227 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ion transport protein | A, B, C, D | protein | 284 | Arcobacter butzleri RM4018 | A8EVM5 (AlphaFold model) |
>6KE5_1 Ion transport protein (chains A, B, C, D) DYKDDDDKGSLVPRGSHMYLRITNIVESSFFTKFIIYLIVLNGITMGLETSKTFMQSFGV YTTLFNQIVITIFTIEIILRIYVHRISFFKDPWSLFDFFVVAISLVPTSSGFEILRVLRV LRLFRLVTAVPQMRKIVSALISVIPGMLSVIALMTLFFYIFAIMATQLFGERFPEWFGTL GESFYTLFQVMTLDDWSNGIVRPLMEVYPYAYVFFIPFIFVVTFVMINLVVAIIVDAMAI LNQKEEQHIIDEVQSHEDNINNEIIKLREEIVELKELIKTSLKN
| ID | Name | Formula | Copies |
|---|---|---|---|
| 6UB | amlodipine | C20 H25 Cl N2 O5 | 1 |
| D6C | [(2~{S},3~{R})-5-[2-(dimethylamino)ethyl]-2-(4-methoxyphenyl)-4-oxidanylidene-2… | C22 H26 N2 O4 S | 1 |
| G3P | Sn-glycerol-3-phosphate | C3 H9 O6 P | 5 |
| CA | Calcium ion | Ca | 3 |
| LPC | [1-myristoyl-glycerol-3-yl]phosphonylcholine | C22 H47 N O7 P | 3 |
Structural Basis for Diltiazem Block of a Voltage-Gated Ca2+Channel. Tang, L., Gamal El-Din, T.M., Lenaeus, M.J. et al. Mol Pharmacol (2019) 96:485-492. DOI 10.1124/mol.119.117531 · PubMed
Other PDB entries of the same protein (UniProt A8EVM5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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