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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：P02647 New Search
31PDB entries
32Biological assembly
82chain/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
1AV1 CRYSTAL STRUCTURE OF HUMAN APOLIPOPROTEIN A-I Deposited 1997-09-23 Assembly 1 Protein homooligomer Homooligomer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 68–267（200 aa） Fragment：LIPID-BINDING DOMAIN
Chain B 68–267（200 aa） Fragment：LIPID-BINDING DOMAIN
Chain C 68–267（200 aa） Fragment：LIPID-BINDING DOMAIN
Chain D 68–267（200 aa） Fragment：LIPID-BINDING DOMAIN
Mutation：N-TERMINAL MET, DEL(1-43) Mutation：N-TERMINAL MET, DEL(1-43) Mutation：N-TERMINAL MET, DEL(1-43) Mutation：N-TERMINAL MET, DEL(1-43) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 7.5；277 K；PROTEIN WAS CRYSTALLIZED FROM 1.2 M NA CITRATE, 100 MM HEPES, PH 7.5 AT 4 DEGREES CELSIUS. CRYSTALS WERE STABILIZED IN 1.4 M NA CITRATE, 100 MM HEPES, PH 7.5., temperature 277K
Resolution 4.00 Å R-free 0.428
1GW3 THE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-I DETERMINED BY NMR SPECTROSCOPY, 1 STRUCTURE Deposited 1997-06-04 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 166–211（46 aa） Fragment：RESIDUES 142 - 187
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.9；310 K
Resolution not provided
1GW4 THE HELIX-HINGE-HELIX STRUCTURAL MOTIF IN HUMAN APOLIPOPROTEIN A-I DETERMINED BY NMR SPECTROSCOPY, 1 STRUCTURE Deposited 1997-06-04 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 166–211（46 aa） Fragment：RESIDUES 142 - 187
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 4.9；323 K
Resolution not provided
1ODP PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 6.6, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40 Deposited 1996-03-02 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 190–209（20 aa） Fragment：RESIDUES 166 - 185
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6.6；310 K
Resolution not provided
1ODQ PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40 Deposited 1996-03-02 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 190–209（20 aa） Fragment：RESIDUES 166 - 185
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.7；310 K
Resolution not provided
1ODR PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 6.0, 37 DEGREES CELSIUS AND PEPTIDE:DPC MOLE RATIO OF 1:40 Deposited 1996-03-02 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 190–209（20 aa） Fragment：RESIDUES 166 - 185
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 6；310 K
Resolution not provided
2MSC NMR data-driven model of GTPase KRas-GDP tethered to a lipid-bilayer nanodisc Deposited 2014-07-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 68–265（198 aa） Fragment：UNP residues 68-265
Chain C 68–265（198 aa） Fragment：UNP residues 68-265
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 1 SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0.105；Pressure ambient
NMR sample composition 20 mM TRIS-1, 100 mM sodium chloride-2, 2 mM TCEP-3, 5 mM MgCl2-4, 0.6 mM U-15N, Ile C-delta-13C K-Ras-5, 0.6 mM membrane scaffold protein-6, 0.6 mM GUANOSINE-5'-DIPHOSPHATE-7, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-8, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-9, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-10, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 20 mM TRIS-11, 100 mM sodium chloride-12, 2 mM TCEP-13, 5 mM Magnesium-14, 0.6 mM U-15N, Ile C-delta-13C K-Ras-15, 0.6 mM membrane scaffold protein-16, 0.6 mM GUANOSINE-5'-DIPHOSPHATE-17, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-18, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-19, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-20, 0.65 mM 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid (gadolinium salt)-21, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2MSD NMR data-driven model of GTPase KRas-GNP tethered to a lipid-bilayer nanodisc Deposited 2014-07-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 68–265（198 aa） Fragment：UNP RESIDUES 68-265
Chain C 68–265（198 aa） Fragment：UNP RESIDUES 68-265
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0.105；Pressure ambient
NMR sample composition 0.6 mM U-15N, Ile C-delta-13C K-Ras-1, 0.6 mM membrane scaffold protein-2, 20 mM TRIS-3, 100 mM sodium chloride-4, 2 mM TCEP-5, 0.6 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-6, 5 mM Magnesium-7, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-8, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-9, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-10, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.6 mM U-15N, Ile C-delta-13C K-Ras-11, 0.6 mM membrane scaffold protein-12, 20 mM TRIS-13, 100 mM sodium chloride-14, 5 mM Magnesium-15, 0.6 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-16, 2 mM TCEP-17, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-18, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-19, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-20, 0.65 mM 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid (gadolinium salt)-21, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2MSE NMR data-driven model of GTPase KRas-GNP:ARafRBD complex tethered to a lipid-bilayer nanodisc Deposited 2014-07-29 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 68–265（198 aa） Fragment：UNP residues 68-265
Chain C 68–265（198 aa） Fragment：UNP residues 68-265
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 0.105；Pressure ambient
NMR sample composition 0.6 mM U-15N, Ile C-delta-13C K-Ras-1, 0.6 mM membrane scaffold protein-2, 0.7 mM A-RafRBD-3, 100 mM sodium chloride-4, 5 mM Magnesium-5, 20 mM TRIS-6, 2 mM TCEP-7, 0.6 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-8, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-9, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-10, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-11, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.7 mM K-Ras-12, 0.7 mM membrane scaffold protein-13, 0.6 mM U-15N, Ile C-delta-13C A-RafRBD-14, 5 mM Magnesium-15, 20 mM TRIS-16, 100 mM sodium chloride-17, 2 mM TCEP-18, 0.7 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-19, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-20, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-21, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-22, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.6 mM U-15N, Ile C-delta-13C K-Ras-23, 0.7 mM A-RafRBD-24, 0.6 mM membrane scaffold protein-25, 20 mM TRIS-26, 100 mM sodium chloride-27, 5 mM Magnesium-28, 2 mM TCEP-29, 0.6 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-30, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-31, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-32, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-33, 0.65 mM 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid (gadolinium salt)-34, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.7 mM K-Ras-35, 0.6 mM U-15N, Ile C-delta-13C A-RafRBD-36, 0.7 mM membrane scaffold protein-37, 20 mM TRIS-38, 100 mM sodium chloride-39, 5 mM Magnesium-40, 2 mM TCEP-41, 0.7 mM PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER-42, 18.75 mM 1,2-dioleoyl-sn-glycero-3-phosphocholine-43, 5 mM 1,2-dioleoyl-sn-glycero-3-phospho-L-serine-44, 1.25 mM 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine-N-[4-(p-maleimidomethyl)cyclohexane-carboxamide]-45, 0.65 mM 1,2-distearoyl-sn-glycero-3-phosphoethanolamine-N-diethylenetriaminepentaacetic acid (gadolinium salt)-46, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
2N5E The 3D solution structure of discoidal high-density lipoprotein particles Deposited 2015-07-15 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 79–267（189 aa）
Chain B 79–267（189 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 7.4；316 K；Ionic strength (raw mmCIF value) 100；Pressure ambient
NMR sample composition 0.5-1.0 mM [U-99% 13C; U-99% 15N] H2O, 1 mM stereospecific Methyl-labeling H2O, 1 mM selective unlabeling H2O, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
3K2S Solution structure of double super helix model Deposited 2009-09-30 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 25–267（243 aa）
Chain B 25–267（243 aa）
Not recorded POV (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate × 200 CLR CHOLESTEROL × 20 SOLUTION SCATTERING mmCIF provides none of the parsed conditions Resolution not provided
3R2P 2.2 Angstrom Crystal Structure of C Terminal Truncated Human Apolipoprotein A-I Reveals the Assembly of HDL by Dimerization. Deposited 2011-03-14 Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric（2） Consistent with protein count
Chain A 25–208（184 aa） Fragment：N-terminal domain (UNP 25-208)
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.6；298 K；0.15M potassium bromide, 30% PEG 2000 MME, pH 6.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.20 Å R-free 0.280
4V6M Structure of the ribosome-SecYE complex in the membrane environment Deposited 2011-02-08 Assembly 1 Protein–RNA Heteromer；Protein × 55 PDB declaration: 60-meric（60） Consistent with all polymers
Chain A0 68–267（200 aa）
Chain A1 68–267（200 aa）
Not recorded PEV (1S)-2-{[(2-AMINOETHOXY)(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL STEARATE × 101 PGV (1R)-2-{[{[(2S)-2,3-DIHYDROXYPROPYL]OXY}(HYDROXY)PHOSPHORYL]OXY}-1-[(PALMITOYLOXY)METHYL]ETHYL (11E)-OCTADEC-11-ENOATE × 32 ELECTRON MICROSCOPY
cryo-EM buffer 20 mM Hepes (pH 7.2), 100 mM KOAc, 10 mM Mg(OAc)2, 1 mM DTT, 250 microg/ml chloramphenicol；pH 7.2；20 mM Hepes (pH 7.2), 100 mM KOAc, 10 mM Mg(OAc)2, 1 mM DTT, 250 microg/ml chloramphenicol
cryo-EM vitrification conditions Cryogen ETHANE；liquid ethane was used as a cryogen
Resolution 7.10 Å
6CC9 NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc Deposited 2018-02-06 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 68–265（198 aa） Fragment：UNP residues 68-265
Chain C 68–265（198 aa） Fragment：UNP residues 68-265
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 EWS (2R,4S)-4-[(5-bromo-1H-indole-3-carbonyl)amino]-2-[(4-chlorophenyl)methyl]piperidin-1-ium × 1 SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 100 mM NaCl；Pressure ambient
NMR sample composition 0.2 mM U-15N, Ile, Leu C-delta-13C, Val C-gamma-13C GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM U-15N, Ile, Leu C-delta-13C, Val C-gamma-13C GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 1 mM Cmpd2, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM [U-15N] GTPase KRas isoform b, 1 mM Cmpd2, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6CCH NMR data-driven model of GTPase KRas-GMPPNP tethered to a nanodisc (E3 state) Deposited 2018-02-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 68–265（198 aa） Fragment：UNP residues 68-265
Chain C 68–265（198 aa） Fragment：UNP residues 68-265
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 105；Pressure 1
NMR sample composition 0.2 mM U-15N, Ile, Leu C-delta-13C, Val C-gamma-13C GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM U-15N, Ile, Leu C-delta-13C, Val C-gamma-13C GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 0.4 mM PE-DTPA-Gd, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6CCX NMR data-driven model of GTPase KRas-GMPPNP:Cmpd2 complex tethered to a nanodisc Deposited 2018-02-07 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 68–265（198 aa） Fragment：UNP residues 68-265
Chain C 68–265（198 aa） Fragment：UNP residues 68-265
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 EWS (2R,4S)-4-[(5-bromo-1H-indole-3-carbonyl)amino]-2-[(4-chlorophenyl)methyl]piperidin-1-ium × 1 SOLUTION NMR
NMR measurement conditions pH 7.4；298 K；Ionic strength (raw mmCIF value) 105；Pressure 1
NMR sample composition 0.2 mM U-15N, Ile, Leu C-delta-13C, Val C-gamma-13C GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM GTPase KRas isoform b, 0.4 mM Membrane Scaffold Protein, 100 mM sodium chloride, 20 mM TRIS, 5 mM magnesium chloride, 2 mM TCEP, 0.2 mM GMPPNP, 12 mM DOPC, 3.2 mM DOPS, 0.8 mM PE-MCC, 0.4 mM PE-DTPA-Gd, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6CLZ MT1-MMP HPX domain with Blade 4 Loop Bound to Nanodiscs Deposited 2018-03-02 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 79–267（189 aa） Fragment：residues 79-267
Chain C 79–267（189 aa） Fragment：residues 79-267
Not recorded PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 218 NA SODIUM ION × 1 CL CHLORIDE ION × 1 SOLUTION NMR
NMR measurement conditions pH 7.2；303 K；Ionic strength (raw mmCIF value) 300；Pressure 1
NMR sample composition 20 mM Tris-HCl, 300 mM NaCl, 0.02 % sodium azide, 93 % H2O, 7 % [U-100% 2H] D2O, 90 uM 2H, 13C, 15N MT1-MMP hemopexin-like domain, 180 uM MSP1D1, 14.4 mM PX4, 93% H2O/7% D2O | 93% H2O/7% D2O
Resolution not provided
6CM1 MT1-MMP HPX Domain with Blade 2 Loop Bound to Nanodiscs Deposited 2018-03-02 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 79–267（189 aa） Fragment：residues 79-267
Chain C 79–267（189 aa） Fragment：residues 79-267
Not recorded PX4 1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 218 NA SODIUM ION × 1 CL CHLORIDE ION × 1 SOLUTION NMR
NMR measurement conditions pH 7.2；303 K；Ionic strength (raw mmCIF value) 300；Pressure 1
NMR sample composition 20 mM Tri-HCl, 300 mM NaCl, 0.02 % sodium azide, 93 % H2O, 7 % [U-100% 2H] D2O, 90 uM 2H, 13C, 15N MT1-MMP hemopexin-like domain, 180 uM MSP1D1, 14.4 mM PX4, 93% H2O/7% D2O | 93% H2O/7% D2O
Resolution not provided
6PTS NMR data-driven model of KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state A) Deposited 2019-07-16 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 68–265（198 aa） Fragment：UNP residues 68-265
Chain C 68–265（198 aa） Fragment：UNP residues 68-265
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 SOLUTION NMR
NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 450；Pressure 1
NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 150；Pressure 1
NMR sample composition 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C KRAS, 0.2 mM U-12C, 14N, 1H RBD-CRD, 0.4 mM U-12C, 14N, 1H MSP, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM U-12C, 14N, 1H KRAS, 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C RBD-CRD, 0.4 mM U-12C, 14N, 1H MSP, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM U-12C, 14N, 1H KRAS, 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C RBD-CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM U-12C, 14N, 1H KRAS, 0.2 mM U-2H; U-15N; Ile Leu C-delta-13C, Val C-gamma-13C RBD-CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM U-15N; Ile C-delta-13C, Met methyl-13C KRAS, 0.5 mM Leu C-delta-13C, Val C-gamma-13C, RBD-CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-99% 15N]; [U-13C]; RBD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.3 mM [U-99% 15N]; [U-13C]; CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6PTW NMR data-driven model of KRas-GMPPNP:RBD-CRD complex tethered to a nanodisc (state B) Deposited 2019-07-16 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 68–265（198 aa） Fragment：UNP residues 68-265
Chain C 68–265（198 aa） Fragment：UNP residues 68-265
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 ZN ZINC ION × 2 SOLUTION NMR
NMR measurement conditions pH 5.5；298 K；Ionic strength (raw mmCIF value) 450；Pressure 1
NMR measurement conditions pH 5.5；308 K；Ionic strength (raw mmCIF value) 150；Pressure 1
NMR sample composition 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N; U-2H] KRAS, 0.2 mM [U-12C; U-14N; U-1H] RBD-CRD, 0.4 mM [U-12C; U-14N; U-1H] MSP, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM [U-12C; U-14N; U-1H] KRAS, 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N; U-2H] RBD-CRD, 0.4 mM [U-12C; U-14N; U-1H] MSP, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N] RBD-CRD, 0.2 mM [U-12C; U-14N; U-1H] KRAS Q43C, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.2 mM [Ile, Leu C-delta-13C; Val C-gamma-13C; U-15N] RBD-CRD, 0.2 mM [U-12C; U-14N; U-1H] KRAS N-term C, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-15N; Ile C-delta-13C; Met methyl-13C] KRAS, 0.5 mM [Leu C-delta-13C; Val C-gamma-13C] RBD-CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-13C; U-15N] RBD, 90% H2O/10% D2O | 90% H2O/10% D2O
NMR sample composition 0.5 mM [U-13C; U-15N] CRD, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6W4E NMR-driven structure of KRAS4B-GTP homodimer on a lipid bilayer nanodisc Deposited 2020-03-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 68–265（198 aa）
Chain D 68–265（198 aa）
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 2 MG MAGNESIUM ION × 2 SOLUTION NMR
NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 100；Pressure 1
NMR sample composition 80 uM ILV 13C-methyl; Lys 15N-amide KRAS4B, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
6W4F NMR-driven structure of KRAS4B-GDP homodimer on a lipid bilayer nanodisc Deposited 2020-03-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 68–265（198 aa）
Chain D 68–265（198 aa）
Not recorded PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 64 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 16 GDP GUANOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 SOLUTION NMR
NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 100；Pressure 1
NMR sample composition 80 uM ILV 13C-methyl; Lys 15N-amide KRAS4B, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
7KJR Cryo-EM structure of SARS-CoV-2 ORF3a Deposited 2020-10-26 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain C 79–267（189 aa） Fragment：UNP residues 79-267
Chain D 79–267（189 aa） Fragment：UNP residues 79-267
Not recorded PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE；1 blot force 5 second wait time 3 second blot time
Resolution 2.08 Å
7RSC NMR-driven structure of the KRAS4B-G12D "alpha-alpha" dimer on a lipid bilayer nanodisc Deposited 2021-08-11 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain D 68–265（198 aa）
Chain E 68–265（198 aa）
Not recorded GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 2 MG MAGNESIUM ION × 2 7Q9 [(2~{R})-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-2-propanoyloxy-propyl] (~{Z})-octadec-9-enoate × 128 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 32 SOLUTION NMR
NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 100；Pressure 1
NMR sample composition 80 uM ILV 13C-methyl; Lys 15N-amide KRAS4B, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
7RSE NMR-driven structure of the KRAS4B-G12D "alpha-beta" dimer on a lipid bilayer nanodisc Deposited 2021-08-11 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain D 68–265（198 aa）
Chain E 68–265（198 aa）
Not recorded GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 2 MG MAGNESIUM ION × 2 7Q9 [(2~{R})-3-[oxidanyl-[2-(trimethyl-$l^{4}-azanyl)ethoxy]phosphoryl]oxy-2-propanoyloxy-propyl] (~{Z})-octadec-9-enoate × 128 17F O-[(S)-({(2R)-2,3-bis[(9Z)-octadec-9-enoyloxy]propyl}oxy)(hydroxy)phosphoryl]-L-serine × 32 SOLUTION NMR
NMR measurement conditions pH 7.4；288 K；Ionic strength (raw mmCIF value) 100；Pressure 1
NMR sample composition 80 uM ILV 13C-methyl; Lys 15N-amide KRAS4B, 90% H2O/10% D2O | 90% H2O/10% D2O
Resolution not provided
8EQS Structure of SARS-CoV-1 Orf3a in late endosome/lysosome-like environment, MSP1D1 nanodisc Deposited 2022-10-09 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain C 79–267（189 aa）
Chain D 79–267（189 aa）
Not recorded PEE 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
8VXJ The crystal structure of human apolipoprotein A-I in complex with Fab 55201 Deposited 2024-02-04 Assembly 1 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain C 25–267（243 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；15% PEG 6000, 0.1 M trisodium citrate-citric acid, pH 5.5, 0.02% NaN3
Resolution 2.70 Å R-free 0.298
8VXJ The crystal structure of human apolipoprotein A-I in complex with Fab 55201 Deposited 2024-02-04 Assembly 2 Protein heterocomplex Heteromer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain D 25–267（243 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 5.5；293 K；15% PEG 6000, 0.1 M trisodium citrate-citric acid, pH 5.5, 0.02% NaN3
Resolution 2.70 Å R-free 0.298
9MXZ Lecithin:Cholesterol Acyltransferase Bound to Apolipoprotein A-I dimer in HDL Deposited 2025-01-21 Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain A 25–267（243 aa）
Chain E 25–267（243 aa）
Not recorded 6PL (4S,7R)-4-HYDROXY-N,N,N-TRIMETHYL-9-OXO-7-[(PALMITOYLOXY)METHYL]-3,5,8-TRIOXA-4-PHOSPHAHEXACOSAN-1-AMINIUM 4-OXIDE × 158 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 9.80 Å
9PVY Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I L90P amyloidosis patient Deposited 2025-08-04 Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 25–267（243 aa）
Chain B 25–267（243 aa）
Chain C 25–267（243 aa）
Chain D 25–267（243 aa）
Chain E 25–267（243 aa）
Chain F 25–267（243 aa）
Chain G 25–267（243 aa）
Chain H 25–267（243 aa）
Chain I 25–267（243 aa）
Chain J 25–267（243 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7；H2O containing 5 mM EDTA
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.15 Å
9PVZ Cryo-EM structure of cardiac amyloid fibril from a variant apolipoprotein A-I R173P amyloidosis patient Deposited 2025-08-04 Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 25–267（243 aa）
Chain B 25–267（243 aa）
Chain C 25–267（243 aa）
Chain D 25–267（243 aa）
Chain E 25–267（243 aa）
Chain F 25–267（243 aa）
Chain G 25–267（243 aa）
Chain H 25–267（243 aa）
Chain I 25–267（243 aa）
Chain J 25–267（243 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7；H2O containing 5 mM EDTA
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.30 Å
9PW3 Cryo-EM structure of renal amyloid fibril from a variant apolipoprotein A-I R173P amyloidosis patient Deposited 2025-08-04 Assembly 1 Protein homooligomer Homooligomer；Protein × 10 PDB declaration: decameric（10） Consistent with protein count
Chain A 25–267（243 aa）
Chain B 25–267（243 aa）
Chain C 25–267（243 aa）
Chain D 25–267（243 aa）
Chain E 25–267（243 aa）
Chain F 25–267（243 aa）
Chain G 25–267（243 aa）
Chain H 25–267（243 aa）
Chain I 25–267（243 aa）
Chain J 25–267（243 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7；H2O containing 5 mM EDTA
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.73 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.