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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

5LDW

Structure of mammalian respiratory Complex I, class1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005743cellular_componentmitochondrial inner membrane
A0006120biological_processmitochondrial electron transport, NADH to ubiquinone
A0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
A0022904biological_processrespiratory electron transport chain
A0045271cellular_componentrespiratory chain complex I
A1902600biological_processproton transmembrane transport
B0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
B0048038molecular_functionquinone binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
C0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
D0003954molecular_functionNADH dehydrogenase activity
D0005739cellular_componentmitochondrion
D0005743cellular_componentmitochondrial inner membrane
D0006120biological_processmitochondrial electron transport, NADH to ubiquinone
D0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
D0016491molecular_functionoxidoreductase activity
D0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
D0019826molecular_functionoxygen sensor activity
D0022008biological_processneurogenesis
D0022904biological_processrespiratory electron transport chain
D0032981biological_processmitochondrial respiratory chain complex I assembly
D0042063biological_processgliogenesis
D0045271cellular_componentrespiratory chain complex I
D0046872molecular_functionmetal ion binding
D0048038molecular_functionquinone binding
D0051287molecular_functionNAD binding
D0051536molecular_functioniron-sulfur cluster binding
D0051539molecular_function4 iron, 4 sulfur cluster binding
D0061351biological_processneural precursor cell proliferation
D0071453biological_processcellular response to oxygen levels
D1902600biological_processproton transmembrane transport
E0016491molecular_functionoxidoreductase activity
F0005743cellular_componentmitochondrial inner membrane
F0006120biological_processmitochondrial electron transport, NADH to ubiquinone
F0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
F0010181molecular_functionFMN binding
F0016491molecular_functionoxidoreductase activity
F0022904biological_processrespiratory electron transport chain
F0045271cellular_componentrespiratory chain complex I
F0046872molecular_functionmetal ion binding
F0051287molecular_functionNAD binding
F0051536molecular_functioniron-sulfur cluster binding
F0051539molecular_function4 iron, 4 sulfur cluster binding
F1902600biological_processproton transmembrane transport
G0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
G0016020cellular_componentmembrane
G0016491molecular_functionoxidoreductase activity
G0042773biological_processATP synthesis coupled electron transport
G0051536molecular_functioniron-sulfur cluster binding
H0003954molecular_functionNADH dehydrogenase activity
H0005743cellular_componentmitochondrial inner membrane
H0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
H0009060biological_processaerobic respiration
H0016020cellular_componentmembrane
H0022904biological_processrespiratory electron transport chain
H0032981biological_processmitochondrial respiratory chain complex I assembly
H0045271cellular_componentrespiratory chain complex I
H1902600biological_processproton transmembrane transport
I0016020cellular_componentmembrane
I0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
I0051539molecular_function4 iron, 4 sulfur cluster binding
J0005739cellular_componentmitochondrion
J0005743cellular_componentmitochondrial inner membrane
J0006120biological_processmitochondrial electron transport, NADH to ubiquinone
J0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
J0022904biological_processrespiratory electron transport chain
J0032981biological_processmitochondrial respiratory chain complex I assembly
J0045271cellular_componentrespiratory chain complex I
J1902600biological_processproton transmembrane transport
K0005743cellular_componentmitochondrial inner membrane
K0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
K0016651molecular_functionoxidoreductase activity, acting on NAD(P)H
K0022904biological_processrespiratory electron transport chain
K0042773biological_processATP synthesis coupled electron transport
K0045271cellular_componentrespiratory chain complex I
K1902600biological_processproton transmembrane transport
L0005743cellular_componentmitochondrial inner membrane
L0006120biological_processmitochondrial electron transport, NADH to ubiquinone
L0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
L0015990biological_processelectron transport coupled proton transport
L0022904biological_processrespiratory electron transport chain
L0032981biological_processmitochondrial respiratory chain complex I assembly
L0042773biological_processATP synthesis coupled electron transport
L0045271cellular_componentrespiratory chain complex I
M0003954molecular_functionNADH dehydrogenase activity
M0005743cellular_componentmitochondrial inner membrane
M0006120biological_processmitochondrial electron transport, NADH to ubiquinone
M0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
M0009060biological_processaerobic respiration
M0015990biological_processelectron transport coupled proton transport
M0022904biological_processrespiratory electron transport chain
M0032981biological_processmitochondrial respiratory chain complex I assembly
M0042773biological_processATP synthesis coupled electron transport
M0045271cellular_componentrespiratory chain complex I
M0048039molecular_functionubiquinone binding
N0005743cellular_componentmitochondrial inner membrane
N0006120biological_processmitochondrial electron transport, NADH to ubiquinone
N0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
N0022904biological_processrespiratory electron transport chain
N0032981biological_processmitochondrial respiratory chain complex I assembly
N0045271cellular_componentrespiratory chain complex I
N1902600biological_processproton transmembrane transport
S0005739cellular_componentmitochondrion
S0005743cellular_componentmitochondrial inner membrane
S0022904biological_processrespiratory electron transport chain
S0031966cellular_componentmitochondrial membrane
S0045271cellular_componentrespiratory chain complex I
T0006633biological_processfatty acid biosynthetic process
U0006633biological_processfatty acid biosynthetic process
V0005739cellular_componentmitochondrion
V0005743cellular_componentmitochondrial inner membrane
V0022904biological_processrespiratory electron transport chain
V0045271cellular_componentrespiratory chain complex I
W0005739cellular_componentmitochondrion
W0005743cellular_componentmitochondrial inner membrane
W0022904biological_processrespiratory electron transport chain
W0032981biological_processmitochondrial respiratory chain complex I assembly
W0045271cellular_componentrespiratory chain complex I
X0006120biological_processmitochondrial electron transport, NADH to ubiquinone
Y0005739cellular_componentmitochondrion
Y0005743cellular_componentmitochondrial inner membrane
Y0006120biological_processmitochondrial electron transport, NADH to ubiquinone
Y0022904biological_processrespiratory electron transport chain
Y0045271cellular_componentrespiratory chain complex I
a0005739cellular_componentmitochondrion
a0005743cellular_componentmitochondrial inner membrane
a0022904biological_processrespiratory electron transport chain
a0045271cellular_componentrespiratory chain complex I
b0005743cellular_componentmitochondrial inner membrane
b0045271cellular_componentrespiratory chain complex I
c0005739cellular_componentmitochondrion
c0045271cellular_componentrespiratory chain complex I
d0005743cellular_componentmitochondrial inner membrane
d0006120biological_processmitochondrial electron transport, NADH to ubiquinone
e0005739cellular_componentmitochondrion
e0005743cellular_componentmitochondrial inner membrane
e0005758cellular_componentmitochondrial intermembrane space
e0022904biological_processrespiratory electron transport chain
e0032981biological_processmitochondrial respiratory chain complex I assembly
e0045271cellular_componentrespiratory chain complex I
f0005739cellular_componentmitochondrion
f0005743cellular_componentmitochondrial inner membrane
f0022904biological_processrespiratory electron transport chain
f0045271cellular_componentrespiratory chain complex I
i0006120biological_processmitochondrial electron transport, NADH to ubiquinone
m0005739cellular_componentmitochondrion
n0006120biological_processmitochondrial electron transport, NADH to ubiquinone
o0005739cellular_componentmitochondrion
o0005743cellular_componentmitochondrial inner membrane
o0005758cellular_componentmitochondrial intermembrane space
o0008137molecular_functionNADH dehydrogenase (ubiquinone) activity
o0022904biological_processrespiratory electron transport chain
o0045271cellular_componentrespiratory chain complex I
o1902600biological_processproton transmembrane transport
q0005739cellular_componentmitochondrion
q0005743cellular_componentmitochondrial inner membrane
q0016020cellular_componentmembrane
q0022904biological_processrespiratory electron transport chain
q0045271cellular_componentrespiratory chain complex I
Functional Information from PDB Data
site_idAC1
Number of Residues10
Detailsbinding site for residue SF4 B 201
ChainResidue
BALA53
DHIS190
BCYS54
BCYS55
BGLY90
BSER118
BCYS119
BCYS149
BPRO150
DARG105
site_idAC2
Number of Residues6
Detailsbinding site for residue FES E 301
ChainResidue
ECYS103
ECYS108
ECYS144
ELEU145
EALA147
ECYS148
site_idAC3
Number of Residues14
Detailsbinding site for residue FMN F 501
ChainResidue
FARG68
FGLY69
FGLY70
FALA71
FASN96
FASP98
FGLY100
FCYS186
FGLY187
FGLU189
FVAL222
FALA223
FASN224
FALA406
site_idAC4
Number of Residues5
Detailsbinding site for residue SF4 F 502
ChainResidue
FCYS359
FGLN361
FCYS362
FCYS365
FCYS405
site_idAC5
Number of Residues8
Detailsbinding site for residue SF4 G 801
ChainResidue
GHIS101
GASP104
GCYS105
GCYS108
GGLN110
GCYS114
GGLN117
GGLY206
site_idAC6
Number of Residues6
Detailsbinding site for residue SF4 G 802
ChainResidue
GCYS153
GILE154
GCYS156
GARG158
GCYS159
GCYS203
site_idAC7
Number of Residues6
Detailsbinding site for residue FES G 803
ChainResidue
GPHE40
GCYS41
GGLY50
GCYS52
GCYS55
GCYS69
site_idAC8
Number of Residues8
Detailsbinding site for residue SF4 I 201
ChainResidue
IHIS65
ICYS87
ICYS116
IILE117
ITYR118
ICYS119
IGLY120
ICYS122
site_idAC9
Number of Residues8
Detailsbinding site for residue SF4 I 202
ChainResidue
ICYS77
IILE78
IALA79
ICYS80
ICYS83
ITYR109
ICYS126
IILE131
site_idAD1
Number of Residues4
Detailsbinding site for residue ZN R 201
ChainResidue
RCYS59
RHIS68
RCYS84
RCYS87
Functional Information from PROSITE/UniProt
site_idPS00012
Number of Residues16
DetailsPHOSPHOPANTETHEINE Phosphopantetheine attachment site. DLGLDSLDQVEIIMAM
ChainResidueDetails
TASP39-MET54
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DIDAEKLMCpqEI
ChainResidueDetails
TASP64-ILE76
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiACKlCEaVCP
ChainResidueDetails
ICYS77-PRO88
ICYS116-PRO127
site_idPS00535
Number of Residues12
DetailsCOMPLEX1_49K Respiratory chain NADH dehydrogenase 49 Kd subunit signature. LHRGtEKLiEyK
ChainResidueDetails
DLEU83-LYS94
site_idPS00542
Number of Residues22
DetailsCOMPLEX1_30K Respiratory chain NADH dehydrogenase 30 Kd subunit signature. EREiwDMFgvffanHpdlRrIL
ChainResidueDetails
CGLU131-LEU152
site_idPS00641
Number of Residues18
DetailsCOMPLEX1_75K_1 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 1. PrfCYherlsvaGnCRmC
ChainResidueDetails
GPRO38-CYS55
site_idPS00642
Number of Residues13
DetailsCOMPLEX1_75K_2 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 2. CPiCDqGGeCdLQ
ChainResidueDetails
GCYS105-GLN117
site_idPS00643
Number of Residues11
DetailsCOMPLEX1_75K_3 Respiratory-chain NADH dehydrogenase 75 Kd subunit signature 3. RCIqCtRCIrF
ChainResidueDetails
GARG152-PHE162
site_idPS00644
Number of Residues16
DetailsCOMPLEX1_51K_1 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 1. GAGAYICGEETALIES
ChainResidueDetails
FGLY180-SER195
site_idPS00645
Number of Residues12
DetailsCOMPLEX1_51K_2 Respiratory-chain NADH dehydrogenase 51 Kd subunit signature 2. ESCGqCtPCReG
ChainResidueDetails
FGLU357-GLY368
site_idPS00667
Number of Residues16
DetailsCOMPLEX1_ND1_1 Respiratory-chain NADH dehydrogenase subunit 1 signature 1. GLLQpIaDAIKLFiKE
ChainResidueDetails
HGLY44-GLU59
site_idPS00668
Number of Residues14
DetailsCOMPLEX1_ND1_2 Respiratory-chain NADH dehydrogenase subunit 1 signature 2. PFDLTEGEseLVs.G
ChainResidueDetails
HPRO197-GLY210
site_idPS01099
Number of Residues19
DetailsCOMPLEX1_24K Respiratory-chain NADH dehydrogenase 24 Kd subunit signature. DklFTlieveCLGaCvnAP
ChainResidueDetails
EASP134-PRO152
site_idPS01150
Number of Residues17
DetailsCOMPLEX1_20K Respiratory-chain NADH dehydrogenase 20 Kd subunit signature. GcDRIVPVDIYvPgCPP
ChainResidueDetails
BGLY135-PRO151
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1238
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues7
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues1
DetailsModified residue: {"description":"Hydroxyarginine","evidences":[{"source":"PubMed","id":"23836892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91WD5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Symmetric dimethylarginine","evidences":[{"source":"PubMed","id":"23836892","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"27509854","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"5LC5","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LDW","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5LDX","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9D6J6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by SRC","evidences":[{"source":"UniProtKB","id":"P19404","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues57
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q91YT0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91YT0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues1
DetailsModified residue: {"description":"Omega-N-methylarginine","evidences":[{"source":"UniProtKB","id":"Q91YT0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues39
DetailsDomain: {"description":"4Fe-4S His(Cys)3-ligated-type","evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q56223","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01184","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q91VD9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00711","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CQ75","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CQ75","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CR21","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues2
DetailsModified residue: {"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1907568","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues75
DetailsDomain: {"description":"Carrier","evidences":[{"source":"PROSITE-ProRule","id":"PRU00258","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues2
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q16718","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q9CPP6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q63362","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"Q9CPP6","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues41
DetailsDomain: {"description":"CHCH 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues30
DetailsMotif: {"description":"Cx9C motif 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues30
DetailsMotif: {"description":"Cx9C motif 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues10
DetailsMotif: {"description":"Cx9C motif 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues10
DetailsMotif: {"description":"Cx9C motif 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"12381726","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17060615","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"7958365","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues44
DetailsDomain: {"description":"CHCH","evidences":[{"source":"PROSITE-ProRule","id":"PRU01150","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues11
DetailsCompositional bias: {"description":"Basic and acidic residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"Q3UIU2","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9Y6M9","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI40
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"Q9CR61","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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