Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

3HR4

Human iNOS Reductase and Calmodulin Complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0010181molecular_functionFMN binding
B0000922cellular_componentspindle pole
B0002027biological_processregulation of heart rate
B0005246molecular_functioncalcium channel regulator activity
B0005509molecular_functioncalcium ion binding
B0005513biological_processdetection of calcium ion
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005654cellular_componentnucleoplasm
B0005737cellular_componentcytoplasm
B0005813cellular_componentcentrosome
B0005819cellular_componentspindle
B0005829cellular_componentcytosol
B0005876cellular_componentspindle microtubule
B0005886cellular_componentplasma membrane
B0007186biological_processG protein-coupled receptor signaling pathway
B0008076cellular_componentvoltage-gated potassium channel complex
B0010856molecular_functionadenylate cyclase activator activity
B0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
B0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
B0016020cellular_componentmembrane
B0016240biological_processautophagosome membrane docking
B0019855molecular_functioncalcium channel inhibitor activity
B0019901molecular_functionprotein kinase binding
B0021762biological_processsubstantia nigra development
B0030017cellular_componentsarcomere
B0031432molecular_functiontitin binding
B0031514cellular_componentmotile cilium
B0031982cellular_componentvesicle
B0032465biological_processregulation of cytokinesis
B0032991cellular_componentprotein-containing complex
B0034704cellular_componentcalcium channel complex
B0035458biological_processcellular response to interferon-beta
B0043209cellular_componentmyelin sheath
B0043539molecular_functionprotein serine/threonine kinase activator activity
B0044305cellular_componentcalyx of Held
B0044325molecular_functiontransmembrane transporter binding
B0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
B0046872molecular_functionmetal ion binding
B0048306molecular_functioncalcium-dependent protein binding
B0051592biological_processresponse to calcium ion
B0055117biological_processregulation of cardiac muscle contraction
B0060291biological_processlong-term synaptic potentiation
B0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
B0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
B0071346biological_processcellular response to type II interferon
B0072542molecular_functionprotein phosphatase activator activity
B0097225cellular_componentsperm midpiece
B0097720biological_processcalcineurin-mediated signaling
B0098901biological_processregulation of cardiac muscle cell action potential
B0099523cellular_componentpresynaptic cytosol
B0140056biological_processorganelle localization by membrane tethering
B0140238biological_processpresynaptic endocytosis
B0141110molecular_functiontransporter inhibitor activity
B1901842biological_processnegative regulation of high voltage-gated calcium channel activity
B1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
B1902494cellular_componentcatalytic complex
B1905913biological_processnegative regulation of calcium ion export across plasma membrane
B1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
C0010181molecular_functionFMN binding
D0000922cellular_componentspindle pole
D0002027biological_processregulation of heart rate
D0005246molecular_functioncalcium channel regulator activity
D0005509molecular_functioncalcium ion binding
D0005513biological_processdetection of calcium ion
D0005515molecular_functionprotein binding
D0005576cellular_componentextracellular region
D0005634cellular_componentnucleus
D0005654cellular_componentnucleoplasm
D0005737cellular_componentcytoplasm
D0005813cellular_componentcentrosome
D0005819cellular_componentspindle
D0005829cellular_componentcytosol
D0005876cellular_componentspindle microtubule
D0005886cellular_componentplasma membrane
D0007186biological_processG protein-coupled receptor signaling pathway
D0008076cellular_componentvoltage-gated potassium channel complex
D0010856molecular_functionadenylate cyclase activator activity
D0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
D0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
D0016020cellular_componentmembrane
D0016240biological_processautophagosome membrane docking
D0019855molecular_functioncalcium channel inhibitor activity
D0019901molecular_functionprotein kinase binding
D0021762biological_processsubstantia nigra development
D0030017cellular_componentsarcomere
D0031432molecular_functiontitin binding
D0031514cellular_componentmotile cilium
D0031982cellular_componentvesicle
D0032465biological_processregulation of cytokinesis
D0032991cellular_componentprotein-containing complex
D0034704cellular_componentcalcium channel complex
D0035458biological_processcellular response to interferon-beta
D0043209cellular_componentmyelin sheath
D0043539molecular_functionprotein serine/threonine kinase activator activity
D0044305cellular_componentcalyx of Held
D0044325molecular_functiontransmembrane transporter binding
D0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
D0046872molecular_functionmetal ion binding
D0048306molecular_functioncalcium-dependent protein binding
D0051592biological_processresponse to calcium ion
D0055117biological_processregulation of cardiac muscle contraction
D0060291biological_processlong-term synaptic potentiation
D0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
D0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
D0071346biological_processcellular response to type II interferon
D0072542molecular_functionprotein phosphatase activator activity
D0097225cellular_componentsperm midpiece
D0097720biological_processcalcineurin-mediated signaling
D0098901biological_processregulation of cardiac muscle cell action potential
D0099523cellular_componentpresynaptic cytosol
D0140056biological_processorganelle localization by membrane tethering
D0140238biological_processpresynaptic endocytosis
D0141110molecular_functiontransporter inhibitor activity
D1901842biological_processnegative regulation of high voltage-gated calcium channel activity
D1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
D1902494cellular_componentcatalytic complex
D1905913biological_processnegative regulation of calcium ion export across plasma membrane
D1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
E0010181molecular_functionFMN binding
F0000922cellular_componentspindle pole
F0002027biological_processregulation of heart rate
F0005246molecular_functioncalcium channel regulator activity
F0005509molecular_functioncalcium ion binding
F0005513biological_processdetection of calcium ion
F0005515molecular_functionprotein binding
F0005576cellular_componentextracellular region
F0005634cellular_componentnucleus
F0005654cellular_componentnucleoplasm
F0005737cellular_componentcytoplasm
F0005813cellular_componentcentrosome
F0005819cellular_componentspindle
F0005829cellular_componentcytosol
F0005876cellular_componentspindle microtubule
F0005886cellular_componentplasma membrane
F0007186biological_processG protein-coupled receptor signaling pathway
F0008076cellular_componentvoltage-gated potassium channel complex
F0010856molecular_functionadenylate cyclase activator activity
F0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
F0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
F0016020cellular_componentmembrane
F0016240biological_processautophagosome membrane docking
F0019855molecular_functioncalcium channel inhibitor activity
F0019901molecular_functionprotein kinase binding
F0021762biological_processsubstantia nigra development
F0030017cellular_componentsarcomere
F0031432molecular_functiontitin binding
F0031514cellular_componentmotile cilium
F0031982cellular_componentvesicle
F0032465biological_processregulation of cytokinesis
F0032991cellular_componentprotein-containing complex
F0034704cellular_componentcalcium channel complex
F0035458biological_processcellular response to interferon-beta
F0043209cellular_componentmyelin sheath
F0043539molecular_functionprotein serine/threonine kinase activator activity
F0044305cellular_componentcalyx of Held
F0044325molecular_functiontransmembrane transporter binding
F0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
F0046872molecular_functionmetal ion binding
F0048306molecular_functioncalcium-dependent protein binding
F0051592biological_processresponse to calcium ion
F0055117biological_processregulation of cardiac muscle contraction
F0060291biological_processlong-term synaptic potentiation
F0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
F0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
F0071346biological_processcellular response to type II interferon
F0072542molecular_functionprotein phosphatase activator activity
F0097225cellular_componentsperm midpiece
F0097720biological_processcalcineurin-mediated signaling
F0098901biological_processregulation of cardiac muscle cell action potential
F0099523cellular_componentpresynaptic cytosol
F0140056biological_processorganelle localization by membrane tethering
F0140238biological_processpresynaptic endocytosis
F0141110molecular_functiontransporter inhibitor activity
F1901842biological_processnegative regulation of high voltage-gated calcium channel activity
F1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
F1902494cellular_componentcatalytic complex
F1905913biological_processnegative regulation of calcium ion export across plasma membrane
F1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
G0010181molecular_functionFMN binding
H0000922cellular_componentspindle pole
H0002027biological_processregulation of heart rate
H0005246molecular_functioncalcium channel regulator activity
H0005509molecular_functioncalcium ion binding
H0005513biological_processdetection of calcium ion
H0005515molecular_functionprotein binding
H0005576cellular_componentextracellular region
H0005634cellular_componentnucleus
H0005654cellular_componentnucleoplasm
H0005737cellular_componentcytoplasm
H0005813cellular_componentcentrosome
H0005819cellular_componentspindle
H0005829cellular_componentcytosol
H0005876cellular_componentspindle microtubule
H0005886cellular_componentplasma membrane
H0007186biological_processG protein-coupled receptor signaling pathway
H0008076cellular_componentvoltage-gated potassium channel complex
H0010856molecular_functionadenylate cyclase activator activity
H0010880biological_processregulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum
H0010881biological_processregulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion
H0016020cellular_componentmembrane
H0016240biological_processautophagosome membrane docking
H0019855molecular_functioncalcium channel inhibitor activity
H0019901molecular_functionprotein kinase binding
H0021762biological_processsubstantia nigra development
H0030017cellular_componentsarcomere
H0031432molecular_functiontitin binding
H0031514cellular_componentmotile cilium
H0031982cellular_componentvesicle
H0032465biological_processregulation of cytokinesis
H0032991cellular_componentprotein-containing complex
H0034704cellular_componentcalcium channel complex
H0035458biological_processcellular response to interferon-beta
H0043209cellular_componentmyelin sheath
H0043539molecular_functionprotein serine/threonine kinase activator activity
H0044305cellular_componentcalyx of Held
H0044325molecular_functiontransmembrane transporter binding
H0046427biological_processpositive regulation of receptor signaling pathway via JAK-STAT
H0046872molecular_functionmetal ion binding
H0048306molecular_functioncalcium-dependent protein binding
H0051592biological_processresponse to calcium ion
H0055117biological_processregulation of cardiac muscle contraction
H0060291biological_processlong-term synaptic potentiation
H0060314biological_processregulation of ryanodine-sensitive calcium-release channel activity
H0060315biological_processnegative regulation of ryanodine-sensitive calcium-release channel activity
H0071346biological_processcellular response to type II interferon
H0072542molecular_functionprotein phosphatase activator activity
H0097225cellular_componentsperm midpiece
H0097720biological_processcalcineurin-mediated signaling
H0098901biological_processregulation of cardiac muscle cell action potential
H0099523cellular_componentpresynaptic cytosol
H0140056biological_processorganelle localization by membrane tethering
H0140238biological_processpresynaptic endocytosis
H0141110molecular_functiontransporter inhibitor activity
H1901842biological_processnegative regulation of high voltage-gated calcium channel activity
H1901844biological_processregulation of cell communication by electrical coupling involved in cardiac conduction
H1902494cellular_componentcatalytic complex
H1905913biological_processnegative regulation of calcium ion export across plasma membrane
H1990456biological_processmitochondrion-endoplasmic reticulum membrane tethering
Functional Information from PDB Data
site_idAC1
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN A 999
ChainResidue
ATHR545
AGLY594
ALEU626
AGLY627
ASER628
ATYR631
AARG633
APHE634
ACYS635
AGLU661
AGLN665
AGLU546
CASN595
CGLY596
CASP597
ATHR547
AGLY548
ALYS549
ASER550
ASER591
ATHR592
APHE593

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA B 201
ChainResidue
BASP20
BASP22
BASP24
BTHR26
BGLU31
BHOH152

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 202
ChainResidue
BASP56
BASP58
BASN60
BTHR62
BGLU67

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 203
ChainResidue
BASP93
BASP95
BASN97
BTYR99
BGLU104

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA B 204
ChainResidue
BASP129
BASP131
BASP133
BGLN135
BGLU140

site_idAC6
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FMN C 999
ChainResidue
CTHR545
CGLU546
CTHR547
CLYS549
CSER550
CSER591
CTHR592
CPHE593
CGLY594
CASN595
CGLY596
CLEU626
CGLY627
CSER628
CTYR631
CARG633
CPHE634
CCYS635
CGLU661
CGLN665

site_idAC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 201
ChainResidue
DASP20
DASP22
DASP24
DTHR26
DGLU31
DHOH162

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 202
ChainResidue
DASP56
DASP58
DASN60
DTHR62
DGLU67
DHOH161

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 203
ChainResidue
DASP93
DASP95
DASN97
DTYR99
DGLU104
DHOH163

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 204
ChainResidue
DASP129
DASP131
DASP133
DGLN135
DGLU140
DHOH157

site_idBC2
Number of Residues22
DetailsBINDING SITE FOR RESIDUE FMN E 999
ChainResidue
ESER628
ETYR631
EARG633
EPHE634
ECYS635
EGLU661
EGLN665
GASN595
GGLY596
GASP597
ETHR545
EGLU546
ETHR547
EGLY548
ELYS549
ESER550
ESER591
ETHR592
EPHE593
EGLY594
ELEU626
EGLY627

site_idBC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA F 201
ChainResidue
FASP20
FASP22
FASP24
FTHR26
FGLU31

site_idBC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA F 202
ChainResidue
FASP56
FASP58
FASN60
FTHR62
FASP64
FGLU67
FHOH158

site_idBC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA F 203
ChainResidue
FASP93
FASP95
FASN97
FTYR99
FGLU104
FHOH154

site_idBC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA F 204
ChainResidue
FASP129
FASP131
FASP133
FGLN135
FGLU140
FHOH152

site_idBC7
Number of Residues20
DetailsBINDING SITE FOR RESIDUE FMN G 999
ChainResidue
GTHR545
GGLU546
GTHR547
GGLY548
GLYS549
GSER550
GSER591
GTHR592
GPHE593
GGLY594
GGLY596
GLEU626
GGLY627
GSER628
GTYR631
GARG633
GPHE634
GCYS635
GGLU661
GGLN665

site_idBC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA H 201
ChainResidue
HASP20
HASP22
HASP24
HTHR26
HGLU31

site_idBC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA H 202
ChainResidue
HASP56
HASP58
HASN60
HTHR62
HASP64
HGLU67

site_idCC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA H 203
ChainResidue
HASP93
HASP95
HASN97
HTYR99
HGLU104

site_idCC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA H 204
ChainResidue
HASP129
HASP131
HASP133
HGLN135
HASN137
HGLU140

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
BASP20-LEU32
BASP56-PHE68
BASP93-LEU105
BASP129-PHE141

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues552
DetailsDomain: {"description":"Flavodoxin-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00088","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues80
DetailsRegion: {"description":"Calmodulin-binding","evidences":[{"source":"PubMed","id":"19737939","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HR4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19737939","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3HR4","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q06518","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine; by PKA","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues140
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues140
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues140
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues40
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25441029","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4UMO","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4V0C","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"29724949","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNN","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6CNO","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues20
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"1474585","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"27564677","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1CLL","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"5J03","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues4
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21406692","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues4
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues4
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues4
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues8
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

PDB statisticsPDBj update infoContact PDBjnumon