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Protein Structures and Oligomeric States

Enter a protein name, UniProt accession or PDB ID. Name searches ask you to confirm the protein identity before related structures are queried.

Current Protein Identity：P05484 New Search
9PDB entries
9Biological assembly
9chain/assembly records
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1DW4 NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: CONSTRAINTS ON DISULPHIDE BRIDGES Deposited 2000-01-24 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–25（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；283 K；Ionic strength (raw mmCIF value) 0；Pressure ambient
NMR sample composition 1 | H2O (10% D2O)
NMR sample composition 1 | D2O
Resolution not provided
1DW5 NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE BRIDGES Deposited 2000-01-24 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–25（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；283 K；Ionic strength (raw mmCIF value) 0；Pressure AMBIENT
NMR sample composition 1
Resolution not provided
1FEO Solution structure of omega-conotoxin MVIIA with C-terminal Gly Deposited 2000-07-21 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–25（25 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；283 K；Pressure ambient
NMR sample composition 2 mM omega-MVIIA-Gly | 93% H2O, 7% D20
NMR sample composition 2 mM omega-MVIIA-Gly U-15N | 93% H2O, 7% D20
Resolution not provided
1MVI N-TYPE CALCIUM CHANNEL BLOCKER, OMEGA-CONOTOXIN MVIIA, NMR, 15 STRUCTURES Deposited 1996-08-02 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–25（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3；293 K
Resolution not provided
1OMG NMR STUDY OF OMEGA-CONOTOXIN MVIIA Deposited 1995-04-26 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 1–25（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1TT3 NMR soulution structure of omega-conotoxin [K10]MVIIA Deposited 2004-06-21 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 46–70（25 aa）
Mutation：R10K Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；293 K；Pressure ambient
NMR measurement conditions pH 3.5；280 K；Pressure ambient
NMR sample composition 2mM [K10]MVIIA, 95% H2O, 5% D2O, DSS | 95% H2O/5% D2O
NMR sample composition 2mM [K10]MVIIA, 100% D2O, DSS | 100% D2O
Resolution not provided
1TTK NMR solution structure of omega-conotoxin MVIIA, a N-type calcium channel blocker Deposited 2004-06-22 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 46–70（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；293 K；Pressure ambient
NMR measurement conditions pH 3.5；280 K；Pressure ambient
NMR sample composition 2mM MVIIA, 95% H2O, D2O, DSS | 95% H2O/5% D2O
NMR sample composition 2mM MVIIA, 100% D2O | 100% D2O
Resolution not provided
7MIX Human N-type voltage-gated calcium channel Cav2.2 in the presence of ziconotide at 3.0 Angstrom resolution Deposited 2021-04-18 Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain B 46–70（25 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 3 CA CALCIUM ION × 2 Y01 CHOLESTEROL HEMISUCCINATE × 2 CLR CHOLESTEROL × 5 3PE 1,2-Distearoyl-sn-glycerophosphoethanolamine × 2 PT5 [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；blot for 6 seconds before plunging
Resolution 3.00 Å
7VFU Human N-type voltage gated calcium channel CaV2.2-alpha2/delta1-beta1 complex, bound to ziconotide Deposited 2021-09-13 Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain E 46–70（25 aa）
Not recorded R16 HEXADECANE × 18 Y01 CHOLESTEROL HEMISUCCINATE × 3 PT5 [(2R)-1-octadecanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phospho ryl]oxy-propan-2-yl] (8Z)-icosa-5,8,11,14-tetraenoate × 1 CA CALCIUM ION × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 8 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å

This page presents structural evidence recorded in PDB/mmCIF.“No recorded non-water small molecule” does not prove that the experimental sample was ligand-free; experimental conditions belong to the PDB experiment, while ligands and copy counts are shown for each biological assembly.