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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：K0BRG7 New Search
23PDB entries
25Biological assembly
67chain/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
4KQZ structure of the receptor binding domain (RBD) of MERS-CoV spike Deposited 2013-05-15 Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain A 367–606（240 aa） Fragment：UNP RESIDUES 367-606
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；0.1M ammonium tartrate dibasic pH7.0, 12% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.51 Å R-free 0.251
4KQZ structure of the receptor binding domain (RBD) of MERS-CoV spike Deposited 2013-05-15 Assembly 2 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric（1） Consistent with protein count
Chain B 367–606（240 aa） Fragment：UNP RESIDUES 367-606
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7；291 K；0.1M ammonium tartrate dibasic pH7.0, 12% PEG 3350, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.51 Å R-free 0.251
4KR0 Complex structure of MERS-CoV spike RBD bound to CD26 Deposited 2013-05-15 Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric（4） Consistent with protein count
Chain B 367–606（240 aa） Fragment：UNP RESIDUES 367-606
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 4.5；291 K；6% v/v 2-propanol, 0.1M sodium acetate pH4.5, 26% PEG 550, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 2.70 Å R-free 0.232
4MOD Structure of the MERS-CoV fusion core Deposited 2013-09-12 Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 992–1054（63 aa）
Chain A 1252–1286（35 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1M BIS-TRIS, 25%(w/v) Polyethylene glycol 3350, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 1.90 Å R-free 0.213
4MOD Structure of the MERS-CoV fusion core Deposited 2013-09-12 Assembly 2 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain B 992–1054（63 aa）
Chain B 1252–1286（35 aa）
Not recorded No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 6.5；291 K；0.1M BIS-TRIS, 25%(w/v) Polyethylene glycol 3350, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K
Resolution 1.90 Å R-free 0.213
6Q04 MERS-CoV S structure in complex with 5-N-acetyl neuraminic acid Deposited 2019-08-01 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 19–1294（1276 aa）
Chain B 19–1294（1276 aa）
Chain C 19–1294（1276 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 FOL FOLIC ACID × 3 SIA N-acetyl-alpha-neuraminic acid × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.50 Å
6Q05 MERS-CoV S structure in complex with sialyl-lewisX Deposited 2019-08-01 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 19–1294（1276 aa）
Chain B 19–1294（1276 aa）
Chain C 19–1294（1276 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 FOL FOLIC ACID × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
6Q06 MERS-CoV S structure in complex with 2,3-sialyl-N-acetyl-lactosamine Deposited 2019-08-01 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 19–1294（1276 aa）
Chain B 19–1294（1276 aa）
Chain C 19–1294（1276 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 21 FOL FOLIC ACID × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.70 Å
6Q07 MERS-CoV S structure in complex with 2,6-sialyl-N-acetyl-lactosamine Deposited 2019-08-01 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 19–1294（1276 aa）
Chain B 19–1294（1276 aa）
Chain C 19–1294（1276 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24 FOL FOLIC ACID × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.90 Å
7V3L MERS S ectodomain trimer in complex with neutralizing antibody 6516 Deposited 2021-08-10 Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric（9） Consistent with protein count
Chain A 1–1290（1290 aa）
Chain B 1–1290（1290 aa）
Chain C 1–1290（1290 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.47 Å
7V5J MERS S ectodomain trimer in complex with neutralizing antibody 0722(state 2) Deposited 2021-08-17 Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric（9） Consistent with protein count
Chain A 18–1206（1189 aa）
Chain B 18–1206（1189 aa）
Chain C 18–1206（1189 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
7V5K MERS S ectodomain trimer in complex with neutralizing antibody 0722 (state 1) Deposited 2021-08-17 Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric（9） Consistent with protein count
Chain A 18–1206（1189 aa）
Chain B 18–1206（1189 aa）
Chain C 18–1206（1189 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.80 Å
7V6N MERS S ectodomain trimer in complex with neutralizing antibody 111 state1 Deposited 2021-08-20 Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric（9） Consistent with protein count
Chain A 18–1206（1189 aa）
Chain B 18–1206（1189 aa）
Chain C 18–1206（1189 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.99 Å
7V6O MERS S ectodomain trimer in complex with neutralizing antibody 111 (state 2) Deposited 2021-08-20 Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric（9） Consistent with protein count
Chain A 18–1206（1189 aa）
Chain B 18–1206（1189 aa）
Chain C 18–1206（1189 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.56 Å
7X25 MERS-CoV spike complex with S41 neutralizing antibody Fab Class4 (2u1d RBD with 3Fab) Deposited 2022-02-25 Assembly 1 Protein heterocomplex Heteromer；Protein × 9 PDB declaration: nonameric（9） Consistent with protein count
Chain G 1–1290（1290 aa）
Chain I 1–1290（1290 aa）
Chain J 1–1290（1290 aa）
Mutation：V1060P, L1061P Mutation：V1060P, L1061P Mutation：V1060P, L1061P No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.49 Å
7X28 MERS-CoV spike complex with S41 neutralizing antibody Fab Class3 (2u1d RBD with 2Fab) Deposited 2022-02-25 Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric（7） Consistent with protein count
Chain F 1–1290（1290 aa）
Chain G 1–1290（1290 aa）
Chain I 1–1290（1290 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.49 Å
7X29 MERS-CoV spike complex with S41 neutralizing antibody Fab Class2 (1u2d RBD with 2Fab) Deposited 2022-02-25 Assembly 1 Protein heterocomplex Heteromer；Protein × 7 PDB declaration: heptameric（7） Consistent with protein count
Chain A 1–1290（1290 aa）
Chain B 1–1290（1290 aa）
Chain C 1–1290（1290 aa）
Mutation：V1060P, l1061P Mutation：V1060P, l1061P Mutation：V1060P, l1061P No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.49 Å
7X2A MERS-CoV spike complex with S41 neutralizing antibody Fab Class1 (1u2d RBD with 1Fab) Deposited 2022-02-25 Assembly 1 Protein heterocomplex Heteromer；Protein × 5 PDB declaration: pentameric（5） Consistent with protein count
Chain A 1–1290（1290 aa）
Chain B 1–1290（1290 aa）
Chain C 1–1290（1290 aa）
Mutation：V1060P, l1061P Mutation：V1060P, l1061P Mutation：V1060P, l1061P No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.2
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 2.49 Å
7YMT Cryo-EM structure of MERS-CoV spike protein, Two RBD-up conformation 2 Deposited 2022-07-29 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 17–1291（1275 aa）
Chain B 17–1291（1275 aa）
Chain C 17–1291（1275 aa）
Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 17 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.
Resolution 6.55 Å
7YMV Cryo-EM structure of MERS-CoV spike protein, Two RBD-up conformation 1 Deposited 2022-07-29 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 17–1291（1275 aa）
Chain B 17–1291（1275 aa）
Chain C 17–1291（1275 aa）
Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 14 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.
Resolution 6.74 Å
7YMW Cryo-EM structure of MERS-CoV spike protein, One RBD-up conformation 4 Deposited 2022-07-29 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 17–1291（1275 aa）
Chain B 17–1291（1275 aa）
Chain C 17–1291（1275 aa）
Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.
Resolution 6.05 Å
7YMX Cryo-EM structure of MERS-CoV spike protein, One RBD-up conformation 2 Deposited 2022-07-29 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 17–1291（1275 aa）
Chain B 17–1291（1275 aa）
Chain C 17–1291（1275 aa）
Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 20 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.
Resolution 4.44 Å
7YMY Cryo-EM structure of MERS-CoV spike protein, One RBD-up conformation 1 Deposited 2022-07-29 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 17–1291（1275 aa）
Chain B 17–1291（1275 aa）
Chain C 17–1291（1275 aa）
Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 19 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.
Resolution 4.96 Å
7YMZ Cryo-EM structure of MERS-CoV spike protein, intermediate conformation Deposited 2022-07-29 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 17–1291（1275 aa）
Chain B 17–1291（1275 aa）
Chain C 17–1291（1275 aa）
Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 12 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.
Resolution 4.39 Å
7YN0 Cryo-EM structure of MERS-CoV spike protein, all RBD-down conformation Deposited 2022-07-29 Assembly 1 Other combination Homooligomer；Protein × 3 PDB declaration: trimeric（3） Consistent with protein count
Chain A 17–1291（1275 aa）
Chain B 17–1291（1275 aa）
Chain C 17–1291（1275 aa）
Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P Mutation：R748A, R751G, V1060P, L1061P NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 24 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.6
cryo-EM vitrification conditions Cryogen ETHANE；blot for 2.5 seconds before plunging; blot force: -1; waiting time: 30s.
Resolution 4.10 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.