Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

6Q9D

CI Peripheral Arm focused refinement from Ovine respiratory SC I+III2

This is a non-PDB format compatible entry.
Functional Information from GO Data
ChainGOidnamespacecontents
A50022904biological_processrespiratory electron transport chain
A60005739cellular_componentmitochondrion
A60005743cellular_componentmitochondrial inner membrane
A60005747cellular_componentmitochondrial respiratory chain complex I
A60006979biological_processresponse to oxidative stress
A60016020cellular_componentmembrane
A60031966cellular_componentmitochondrial membrane
A60032981biological_processmitochondrial respiratory chain complex I assembly
A60070469cellular_componentrespirasome
A70005743cellular_componentmitochondrial inner membrane
A70005747cellular_componentmitochondrial respiratory chain complex I
A70006120biological_processmitochondrial electron transport, NADH to ubiquinone
A70016020cellular_componentmembrane
A70042773biological_processATP synthesis coupled electron transport
AA0006633biological_processfatty acid biosynthetic process
AL0016020cellular_componentmembrane
AL0032981biological_processmitochondrial respiratory chain complex I assembly
S10008137molecular_functionNADH dehydrogenase (ubiquinone) activity
S10016020cellular_componentmembrane
S10016491molecular_functionoxidoreductase activity
S10016651molecular_functionoxidoreductase activity, acting on NAD(P)H
S10042773biological_processATP synthesis coupled electron transport
S10051536molecular_functioniron-sulfur cluster binding
S20016651molecular_functionoxidoreductase activity, acting on NAD(P)H
S20048038molecular_functionquinone binding
S20051287molecular_functionNAD binding
S30008137molecular_functionNADH dehydrogenase (ubiquinone) activity
S30016651molecular_functionoxidoreductase activity, acting on NAD(P)H
S40022900biological_processelectron transport chain
S60005747cellular_componentmitochondrial respiratory chain complex I
S60006120biological_processmitochondrial electron transport, NADH to ubiquinone
S70008137molecular_functionNADH dehydrogenase (ubiquinone) activity
S70048038molecular_functionquinone binding
S70051536molecular_functioniron-sulfur cluster binding
S70051539molecular_function4 iron, 4 sulfur cluster binding
S80016020cellular_componentmembrane
S80016651molecular_functionoxidoreductase activity, acting on NAD(P)H
S80051539molecular_function4 iron, 4 sulfur cluster binding
V10003954molecular_functionNADH dehydrogenase activity
V10005739cellular_componentmitochondrion
V10005743cellular_componentmitochondrial inner membrane
V10005747cellular_componentmitochondrial respiratory chain complex I
V10006120biological_processmitochondrial electron transport, NADH to ubiquinone
V10008137molecular_functionNADH dehydrogenase (ubiquinone) activity
V10010181molecular_functionFMN binding
V10016020cellular_componentmembrane
V10045271cellular_componentrespiratory chain complex I
V10046872molecular_functionmetal ion binding
V10051287molecular_functionNAD binding
V10051536molecular_functioniron-sulfur cluster binding
V10051539molecular_function4 iron, 4 sulfur cluster binding
V10055085biological_processtransmembrane transport
V10070469cellular_componentrespirasome
V20016491molecular_functionoxidoreductase activity
V30005739cellular_componentmitochondrion
V30005747cellular_componentmitochondrial respiratory chain complex I
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue SF4 V1 500
ChainResidue
V1PRO203
V1CYS405
V1SER358
V1CYS359
V1GLY360
V1GLN361
V1CYS362
V1CYS365
V1THR403
V1ILE404

site_idAC2
Number of Residues14
Detailsbinding site for residue FMN V1 501
ChainResidue
V1GLY67
V1ARG68
V1GLY69
V1ALA71
V1PHE73
V1LYS78
V1ASN96
V1ASP98
V1TYR184
V1GLY187
V1GLU188
V1VAL222
V1ASN224
V1THR227

site_idAC3
Number of Residues8
Detailsbinding site for residue FES V2 300
ChainResidue
V2CYS103
V2THR105
V2CYS108
V2CYS144
V2LEU145
V2GLY146
V2ALA147
V2CYS148

site_idAC4
Number of Residues8
Detailsbinding site for residue SF4 S1 801
ChainResidue
S1HIS101
S1ASP104
S1CYS105
S1CYS108
S1CYS114
S1GLN117
S1VAL205
S1GLY206

site_idAC5
Number of Residues7
Detailsbinding site for residue SF4 S1 802
ChainResidue
S1CYS153
S1ILE154
S1CYS156
S1THR157
S1CYS159
S1CYS203
S1VAL205

site_idAC6
Number of Residues7
Detailsbinding site for residue FES S1 803
ChainResidue
S1CYS41
S1TYR42
S1GLY50
S1CYS52
S1ARG53
S1CYS55
S1CYS69

site_idAC7
Number of Residues10
Detailsbinding site for residue SF4 S7 300
ChainResidue
S2ARG105
S7ALA53
S7CYS54
S7CYS55
S7GLY90
S7GLY117
S7SER118
S7CYS119
S7CYS149
S7PRO150

site_idAC8
Number of Residues10
Detailsbinding site for residue SF4 S8 201
ChainResidue
S8CYS87
S8PRO88
S8ILE92
S8CYS116
S8ILE117
S8TYR118
S8CYS119
S8GLY120
S8CYS122
S8GLU133

site_idAC9
Number of Residues8
Detailsbinding site for residue SF4 S8 202
ChainResidue
S8CYS77
S8ILE78
S8ALA79
S8CYS80
S8LYS81
S8CYS83
S8CYS126
S8ILE131

site_idAD1
Number of Residues5
Detailsbinding site for residue ZN S6 300
ChainResidue
S6CYS59
S6HIS68
S6VAL71
S6CYS84
S6CYS87

site_idAD2
Number of Residues15
Detailsbinding site for residue NDP A9 401
ChainResidue
A9ALA169
A9ILE171
A9ARG177
A9THR27
A9GLY28
A9PHE29
A9LEU30
A9ARG50
A9VAL95
A9GLY96
A9ARG97
A9ILE132
A9HIS134
A9TYR145
A9LYS149

site_idAD3
Number of Residues10
Detailsbinding site for residue ZMP AA 101
ChainResidue
A6LYS28
A6ARG32
A6TRP38
A6VAL62
A6PHE66
A6ASN69
A6ALA70
A6LEU81
AAASP43
AASER44

Functional Information from PROSITE/UniProt
site_idPS00641
Number of Residues18
DetailsCOMPLEX1_75K_1 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. PrfCYherlsvaGnCRmC
ChainResidueDetails
S1PRO38-CYS55

site_idPS00642
Number of Residues13
DetailsCOMPLEX1_75K_2 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. CPiCDqGGeCdLQ
ChainResidueDetails
S1CYS105-GLN117

site_idPS00643
Number of Residues11
DetailsCOMPLEX1_75K_3 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. RCIqCtRCIrF
ChainResidueDetails
S1ARG152-PHE162

site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiACKlCEaVCP
ChainResidueDetails
S8CYS77-PRO88
S8CYS116-PRO127

site_idPS01099
Number of Residues19
DetailsCOMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DklFTlieveCLGaCvnAP
ChainResidueDetails
V2ASP134-PRO152

site_idPS01150
Number of Residues17
DetailsCOMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. GcDRIVPVDIYvPgCPP
ChainResidueDetails
S7GLY135-PRO151

site_idPS00542
Number of Residues22
DetailsCOMPLEX1_30K Respiratory chain NADH dehydrogenase 30 Kd subunit signature. EREiwDMFgvffanHpdlRrIL
ChainResidueDetails
S3GLU131-LEU152

site_idPS00644
Number of Residues16
DetailsCOMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALIES
ChainResidueDetails
V1GLY180-SER195

site_idPS00645
Number of Residues12
DetailsCOMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGqCtPCReG
ChainResidueDetails
V1GLU357-GLY368

site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGLDSLDQVEIIMAM
ChainResidueDetails
AAASP39-MET54

site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DIDAEKLMCpqEI
ChainResidueDetails
AAASP64-ILE76

site_idPS00535
Number of Residues12
DetailsCOMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. LHRGtEKLiEyK
ChainResidueDetails
S2LEU83-LYS94

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon