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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9UPG

Cryo-EM structure of human olfactory CNGA2/A4/B1 in CaM-bound closed state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005216molecular_functionmonoatomic ion channel activity
A0005222molecular_functionintracellularly cAMP-activated cation channel activity
A0005223molecular_functionintracellularly cGMP-activated cation channel activity
A0005262molecular_functioncalcium channel activity
A0005516molecular_functioncalmodulin binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0006814biological_processsodium ion transport
A0006816biological_processcalcium ion transport
A0007606biological_processsensory perception of chemical stimulus
A0007608biological_processsensory perception of smell
A0017071cellular_componentintracellular cyclic nucleotide activated cation channel complex
A0030552molecular_functioncAMP binding
A0030553molecular_functioncGMP binding
A0030660cellular_componentGolgi-associated vesicle membrane
A0034220biological_processmonoatomic ion transmembrane transport
A0060170cellular_componentciliary membrane
A0070588biological_processcalcium ion transmembrane transport
A0098655biological_processmonoatomic cation transmembrane transport
A0098804cellular_componentnon-motile cilium membrane
B0000166molecular_functionnucleotide binding
B0001750cellular_componentphotoreceptor outer segment
B0001895biological_processretina homeostasis
B0005222molecular_functionintracellularly cAMP-activated cation channel activity
B0005223molecular_functionintracellularly cGMP-activated cation channel activity
B0005262molecular_functioncalcium channel activity
B0005272molecular_functionsodium channel activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006812biological_processmonoatomic cation transport
B0006813biological_processpotassium ion transport
B0006814biological_processsodium ion transport
B0006816biological_processcalcium ion transport
B0007186biological_processG protein-coupled receptor signaling pathway
B0007601biological_processvisual perception
B0007608biological_processsensory perception of smell
B0015276molecular_functionligand-gated monoatomic ion channel activity
B0016020cellular_componentmembrane
B0017071cellular_componentintracellular cyclic nucleotide activated cation channel complex
B0021630biological_processolfactory nerve maturation
B0030552molecular_functioncAMP binding
B0030553molecular_functioncGMP binding
B0030660cellular_componentGolgi-associated vesicle membrane
B0034220biological_processmonoatomic ion transmembrane transport
B0035725biological_processsodium ion transmembrane transport
B0043195cellular_componentterminal bouton
B0043855molecular_functioncyclic nucleotide-activated monoatomic ion channel activity
B0044877molecular_functionprotein-containing complex binding
B0050908biological_processdetection of light stimulus involved in visual perception
B0050911biological_processdetection of chemical stimulus involved in sensory perception of smell
B0051480biological_processregulation of cytosolic calcium ion concentration
B0051899biological_processmembrane depolarization
B0060170cellular_componentciliary membrane
B0070588biological_processcalcium ion transmembrane transport
B0098655biological_processmonoatomic cation transmembrane transport
B0098804cellular_componentnon-motile cilium membrane
B0120200cellular_componentrod photoreceptor outer segment
B1902495cellular_componenttransmembrane transporter complex
B1990834biological_processresponse to odorant
C0000166molecular_functionnucleotide binding
C0005216molecular_functionmonoatomic ion channel activity
C0005222molecular_functionintracellularly cAMP-activated cation channel activity
C0005223molecular_functionintracellularly cGMP-activated cation channel activity
C0005262molecular_functioncalcium channel activity
C0005516molecular_functioncalmodulin binding
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006813biological_processpotassium ion transport
C0006814biological_processsodium ion transport
C0006816biological_processcalcium ion transport
C0007606biological_processsensory perception of chemical stimulus
C0007608biological_processsensory perception of smell
C0017071cellular_componentintracellular cyclic nucleotide activated cation channel complex
C0030552molecular_functioncAMP binding
C0030553molecular_functioncGMP binding
C0030660cellular_componentGolgi-associated vesicle membrane
C0034220biological_processmonoatomic ion transmembrane transport
C0060170cellular_componentciliary membrane
C0070588biological_processcalcium ion transmembrane transport
C0098655biological_processmonoatomic cation transmembrane transport
C0098804cellular_componentnon-motile cilium membrane
D0000166molecular_functionnucleotide binding
D0005222molecular_functionintracellularly cAMP-activated cation channel activity
D0005223molecular_functionintracellularly cGMP-activated cation channel activity
D0005262molecular_functioncalcium channel activity
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0006813biological_processpotassium ion transport
D0006814biological_processsodium ion transport
D0006816biological_processcalcium ion transport
D0007606biological_processsensory perception of chemical stimulus
D0007608biological_processsensory perception of smell
D0017071cellular_componentintracellular cyclic nucleotide activated cation channel complex
D0030552molecular_functioncAMP binding
D0030553molecular_functioncGMP binding
D0030660cellular_componentGolgi-associated vesicle membrane
D0034220biological_processmonoatomic ion transmembrane transport
D0060170cellular_componentciliary membrane
D0070588biological_processcalcium ion transmembrane transport
D0098655biological_processmonoatomic cation transmembrane transport
D0098804cellular_componentnon-motile cilium membrane
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 PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DKDGDGTITtkEL
ChainResidueDetails
HASP21-LEU33
HASP57-PHE69
HASP94-LEU106
HASP130-PHE142
site_idPS00888
Number of Residues17
DetailsCNMP_BINDING_1 Cyclic nucleotide-binding domain signature 1. VCrKGDiGQeMYIIreG
ChainResidueDetails
DVAL375-GLY391
BVAL989-GLY1005
AILE481-GLY497
site_idPS00889
Number of Residues24
DetailsCNMP_BINDING_2 Cyclic nucleotide-binding domain signature 2. FGEiSIinikgnmsgnrRTAnIkS
ChainResidueDetails
DPHE413-SER436
BPHE1028-ALA1048
APHE519-SER542
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsTransmembrane: {"description":"Helical; Name=S1","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues135
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues60
DetailsTransmembrane: {"description":"Helical; Name=S2","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues115
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues54
DetailsTransmembrane: {"description":"Helical; Name=S4","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues69
DetailsTransmembrane: {"description":"Helical; Name=S5","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues102
DetailsTransmembrane: {"description":"Helical; Name=P-helix","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues72
DetailsTransmembrane: {"description":"Helical; Name=S6","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues324
DetailsRegion: {"description":"Ion conduction pathway","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues9
DetailsRegion: {"description":"Selectivity filter","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues228
DetailsRegion: {"description":"C-linker","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI12
Number of Residues360
DetailsRegion: {"description":"Cyclic nucleotide-binding domain","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI13
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI14
Number of Residues5
DetailsSite: {"description":"Central gate","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=S3","evidences":[{"source":"UniProtKB","id":"P29973","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues10
DetailsMotif: {"description":"IQ-type"}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S1","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=S2","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues19
DetailsTransmembrane: {"description":"Helical; Name=S3","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI20
Number of Residues12
DetailsTransmembrane: {"description":"Helical; Name=S4","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI21
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=S5","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI22
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=P-helix","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI23
Number of Residues25
DetailsTransmembrane: {"description":"Helical; Name=S6","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RH9","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI24
Number of Residues10
DetailsRegion: {"description":"Calmodulin-binding CaM1","evidences":[{"source":"UniProtKB","id":"Q28181","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI25
Number of Residues99
DetailsRegion: {"description":"Ion conduction pathway","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI26
Number of Residues76
DetailsRegion: {"description":"C-linker","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI27
Number of Residues116
DetailsRegion: {"description":"Cyclic nucleotide-binding domain","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"7RHI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI28
Number of Residues10
DetailsMotif: {"description":"IQ-like"}
ChainResidueDetails
site_idSWS_FT_FI29
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RHI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI30
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RHH","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI31
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RHH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7RHI","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI32
Number of Residues2
DetailsSite: {"description":"Central gate","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI33
Number of Residues1
DetailsSite: {"description":"Occludes the pore below the central gate","evidences":[{"source":"PubMed","id":"34699778","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails
site_idSWS_FT_FI34
Number of Residues35
DetailsDomain: {"description":"EF-hand 1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI35
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI36
Number of Residues35
DetailsDomain: {"description":"EF-hand 3","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI37
Number of Residues32
DetailsDomain: {"description":"EF-hand 4","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI38
Number of Residues72
DetailsRegion: {"description":"Necessary and sufficient for interaction with PCP4","evidences":[{"source":"PubMed","id":"27876793","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI39
Number of Residues10
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_FI40
Number of Residues5
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_FI41
Number of Residues5
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_FI42
Number of Residues1
DetailsModified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"7093203","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"FEB-2008","submissionDatabase":"UniProtKB","authors":["Bienvenut W.V.","Bensaad K.","Vousden K.H."]}},{"source":"PubMed","id":"19413330","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI43
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI44
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by CaMK4","evidences":[{"source":"UniProtKB","id":"P0DP29","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI45
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI46
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI47
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18669648","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI48
Number of Residues1
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_FI49
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"24275569","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI50
Number of Residues1
DetailsModified residue: {"description":"N6-methyllysine; alternate","evidences":[{"source":"PubMed","id":"24129315","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI51
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI52
Number of Residues2
DetailsCross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate","evidences":[{"source":"UniProtKB","id":"P62157","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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