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3IYL

Atomic CryoEM Structure of a Nonenveloped Virus Suggests How Membrane Penetration Protein is Primed for Cell Entry

Functional Information from GO Data
ChainGOidnamespacecontents
A0039624cellular_componentviral outer capsid
A0046718biological_processsymbiont entry into host cell
A0046812molecular_functionhost cell surface binding
B0039624cellular_componentviral outer capsid
B0046718biological_processsymbiont entry into host cell
B0046812molecular_functionhost cell surface binding
C0039624cellular_componentviral outer capsid
C0046718biological_processsymbiont entry into host cell
C0046812molecular_functionhost cell surface binding
D0039624cellular_componentviral outer capsid
D0046718biological_processsymbiont entry into host cell
D0046812molecular_functionhost cell surface binding
E0039624cellular_componentviral outer capsid
E0046718biological_processsymbiont entry into host cell
E0046812molecular_functionhost cell surface binding
F0039624cellular_componentviral outer capsid
F0046718biological_processsymbiont entry into host cell
F0046812molecular_functionhost cell surface binding
G0039624cellular_componentviral outer capsid
G0046718biological_processsymbiont entry into host cell
G0046812molecular_functionhost cell surface binding
H0039624cellular_componentviral outer capsid
H0046718biological_processsymbiont entry into host cell
H0046812molecular_functionhost cell surface binding
I0039624cellular_componentviral outer capsid
I0046718biological_processsymbiont entry into host cell
I0046812molecular_functionhost cell surface binding
J0039624cellular_componentviral outer capsid
J0046718biological_processsymbiont entry into host cell
J0046812molecular_functionhost cell surface binding
K0039624cellular_componentviral outer capsid
K0046718biological_processsymbiont entry into host cell
K0046812molecular_functionhost cell surface binding
L0039624cellular_componentviral outer capsid
L0046718biological_processsymbiont entry into host cell
L0046812molecular_functionhost cell surface binding
M0039624cellular_componentviral outer capsid
M0046718biological_processsymbiont entry into host cell
M0046812molecular_functionhost cell surface binding
N0039624cellular_componentviral outer capsid
N0046718biological_processsymbiont entry into host cell
N0046812molecular_functionhost cell surface binding
O0039624cellular_componentviral outer capsid
O0046718biological_processsymbiont entry into host cell
O0046812molecular_functionhost cell surface binding
P0039624cellular_componentviral outer capsid
P0046718biological_processsymbiont entry into host cell
P0046812molecular_functionhost cell surface binding
Q0039624cellular_componentviral outer capsid
Q0046718biological_processsymbiont entry into host cell
Q0046812molecular_functionhost cell surface binding
R0039624cellular_componentviral outer capsid
R0046718biological_processsymbiont entry into host cell
R0046812molecular_functionhost cell surface binding
S0039624cellular_componentviral outer capsid
S0046718biological_processsymbiont entry into host cell
S0046812molecular_functionhost cell surface binding
T0039624cellular_componentviral outer capsid
T0046718biological_processsymbiont entry into host cell
T0046812molecular_functionhost cell surface binding
W0004482molecular_functionmRNA 5'-cap (guanine-N7-)-methyltransferase activity
W0004484molecular_functionmRNA guanylyltransferase activity
W0005524molecular_functionATP binding
W0006370biological_process7-methylguanosine mRNA capping
W0019028cellular_componentviral capsid
X0003724molecular_functionRNA helicase activity
X0016787molecular_functionhydrolase activity
Y0003724molecular_functionRNA helicase activity
Y0016787molecular_functionhydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR A 649
ChainResidue
AGLY2
BALA211
AILE13
BLEU163
BMET167
BLEU187
BLYS191
BCYS200
BPRO204
BTYR208

site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR C 649
ChainResidue
CGLY2
CILE13
DLEU163
DMET167
DLEU187
DLYS191
DCYS200
DPRO204
DTYR208
DALA211

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR E 649
ChainResidue
EGLY2
EILE13
FLEU163
FMET167
FLEU187
FLYS191
FCYS200
FPRO204
FTYR208
FALA211

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR G 649
ChainResidue
GGLY2
GILE13
HLEU163
HMET167
HLEU187
HLYS191
HCYS200
HPRO204
HTYR208
HALA211

site_idAC5
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR I 649
ChainResidue
IGLY2
IILE13
JLEU163
JMET167
JLEU187
JLYS191
JCYS200
JPRO204
JTYR208
JALA211

site_idAC6
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR K 649
ChainResidue
KGLY2
KILE13
LLEU163
LMET167
LLEU187
LLYS191
LCYS200
LPRO204
LTYR208
LALA211

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR M 649
ChainResidue
MGLY2
MILE13
NLEU163
NMET167
NLEU187
NLYS191
NCYS200
NPRO204
NTYR208
NALA211

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR O 649
ChainResidue
OGLY2
OILE13
PLEU163
PMET167
PLEU187
PLYS191
PCYS200
PPRO204
PTYR208
PALA211

site_idAC9
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR Q 649
ChainResidue
QGLY2
QILE13
RLEU163
RMET167
RLEU187
RLYS191
RCYS200
RPRO204
RTYR208
RALA211

site_idBC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE MYR S 649
ChainResidue
TALA211
SGLY2
SILE13
TLEU163
TMET167
TLEU187
TLYS191
TCYS200
TPRO204
TTYR208

Functional Information from PROSITE/UniProt
site_idPS00028
Number of Residues22
DetailsZINC_FINGER_C2H2_1 Zinc finger C2H2 type domain signature. Cnv..CnarFstmsalseHlrsd.H
ChainResidueDetails
XCYS119-HIS140

221716

PDB entries from 2024-06-26

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