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6RD5

CryoEM structure of Polytomella F-ATP synthase, focussed refinement of Fo and peripheral stalk, C2 symmetry

Functional Information from GO Data
ChainGOidnamespacecontents
00016020cellular_componentmembrane
10005739cellular_componentmitochondrion
80016020cellular_componentmembrane
90016020cellular_componentmembrane
M0006754biological_processATP biosynthetic process
M0009579cellular_componentthylakoid
M0015078molecular_functionproton transmembrane transporter activity
M0015986biological_processproton motive force-driven ATP synthesis
M0016020cellular_componentmembrane
M0045263cellular_componentproton-transporting ATP synthase complex, coupling factor F(o)
M1902600biological_processproton transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues13
Detailsbinding site for residue PEV 0 101
ChainResidue
0GLN13
6GLN74
8PHE32
8PEV104
MARG98
0PRO15
0ALA16
0LEU18
0SER19
0PEV102
0PEV103
5SER20
5TRP24

site_idAC2
Number of Residues9
Detailsbinding site for residue PEV 0 102
ChainResidue
0ALA20
0CYS31
0THR32
0ARG34
0PEV101
5SER7
5GLN9
5VAL17
8THR52

site_idAC3
Number of Residues12
Detailsbinding site for residue PEV 0 103
ChainResidue
0GLY11
0PHE12
0PEV101
1PEV701
6GLY70
6SER72
6ALA75
6ILE77
6ALA78
6GLY81
6SER117
9PEV102

site_idAC4
Number of Residues7
Detailsbinding site for residue PEV 1 701
ChainResidue
0PEV103
1SER322
1SER323
1PHE324
1LEU325
1LYS327
9PEV102

site_idAC5
Number of Residues9
Detailsbinding site for residue LMT 6 201
ChainResidue
6GLY131
6MET132
6PRO134
6ALA137
6LMT202
MGLY112
MARG115
MPHE116
MLMT404

site_idAC6
Number of Residues5
Detailsbinding site for residue LMT 6 202
ChainResidue
6ALA128
6MET132
6LMT201
6PEV205
MLMT404

site_idAC7
Number of Residues5
Detailsbinding site for residue PEV 6 203
ChainResidue
6TRP112
6LEU119
9HIS41
MCYS279
MALA283

site_idAC8
Number of Residues6
Detailsbinding site for residue PEV 6 204
ChainResidue
0ASN29
6GLY81
6TRP85
6TYR88
MASN171
MGLU172

site_idAC9
Number of Residues6
Detailsbinding site for residue PEV 6 205
ChainResidue
1SER323
6ALA124
6ALA128
6PHE129
6LMT202
MLEU105

site_idAD1
Number of Residues6
Detailsbinding site for residue LMT 8 101
ChainResidue
8PRO42
8TRP45
8GLY49
8THR56
8PEV104
MPHE202

site_idAD2
Number of Residues3
Detailsbinding site for residue PEV 8 102
ChainResidue
8TYR58
8LEU64
8LYS71

site_idAD3
Number of Residues2
Detailsbinding site for residue LMT 8 103
ChainResidue
8GLY59
8LEU64

site_idAD4
Number of Residues6
Detailsbinding site for residue PEV 8 104
ChainResidue
0PEV101
8SER31
8PHE32
8TYR33
8THR37
8LMT101

site_idAD5
Number of Residues6
Detailsbinding site for residue LMT 9 101
ChainResidue
0ALA64
0PHE65
0LYS67
9ALA55
9ASN56
MPHE170

site_idAD6
Number of Residues11
Detailsbinding site for residue PEV 9 102
ChainResidue
6SER117
9THR4
9LEU7
9GLY8
9PHE11
9PHE18
9LMT103
0PEV103
1PHE324
1PEV701
6GLY70

site_idAD7
Number of Residues8
Detailsbinding site for residue LMT 9 103
ChainResidue
6ILE114
6SER117
6SER118
9TYR14
9PHE15
9VAL37
9ARG40
9PEV102

site_idAD8
Number of Residues3
Detailsbinding site for residue ZN M 401
ChainResidue
6HOH310
MHIS248
MHIS252

site_idAD9
Number of Residues9
Detailsbinding site for residue PEV M 402
ChainResidue
0PHE12
0GLN13
5TRP21
5GLN29
5LEU30
MARG98
MVAL100
MPRO106
MTHR107

site_idAE1
Number of Residues5
Detailsbinding site for residue LMT M 403
ChainResidue
MPHE116
MGLN120
MASN121
MILE301
MLMT404

site_idAE2
Number of Residues6
Detailsbinding site for residue LMT M 404
ChainResidue
6LMT201
6LMT202
MARG115
MPHE116
MSER119
MLMT403

Functional Information from PROSITE/UniProt
site_idPS00449
Number of Residues10
DetailsATPASE_A ATP synthase a subunit signature. SLGVRLWVNM
ChainResidueDetails
MSER235-MET244

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PDB entries from 2024-07-24

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