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7DXH

Cryo-EM structure of PSII intermediate Psb28-PSII complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0009523cellular_componentphotosystem II
A0009654cellular_componentphotosystem II oxygen evolving complex
A0015979biological_processphotosynthesis
A0016020cellular_componentmembrane
A0031676cellular_componentplasma membrane-derived thylakoid membrane
A0042651cellular_componentthylakoid membrane
B0009523cellular_componentphotosystem II
B0015979biological_processphotosynthesis
B0031676cellular_componentplasma membrane-derived thylakoid membrane
a0005506molecular_functioniron ion binding
a0009055molecular_functionelectron transfer activity
a0009523cellular_componentphotosystem II
a0009635biological_processresponse to herbicide
a0009772biological_processphotosynthetic electron transport in photosystem II
a0010242molecular_functionoxygen evolving activity
a0015979biological_processphotosynthesis
a0016168molecular_functionchlorophyll binding
a0016491molecular_functionoxidoreductase activity
a0016682molecular_functionoxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor
a0019684biological_processphotosynthesis, light reaction
a0031676cellular_componentplasma membrane-derived thylakoid membrane
a0042651cellular_componentthylakoid membrane
a0046872molecular_functionmetal ion binding
b0009521cellular_componentphotosystem
b0009523cellular_componentphotosystem II
b0009767biological_processphotosynthetic electron transport chain
b0009772biological_processphotosynthetic electron transport in photosystem II
b0015979biological_processphotosynthesis
b0016020cellular_componentmembrane
b0016168molecular_functionchlorophyll binding
b0019684biological_processphotosynthesis, light reaction
b0031676cellular_componentplasma membrane-derived thylakoid membrane
b0046872molecular_functionmetal ion binding
c0005737cellular_componentcytoplasm
c0009521cellular_componentphotosystem
c0009523cellular_componentphotosystem II
c0009767biological_processphotosynthetic electron transport chain
c0009772biological_processphotosynthetic electron transport in photosystem II
c0015979biological_processphotosynthesis
c0016020cellular_componentmembrane
c0016168molecular_functionchlorophyll binding
c0019684biological_processphotosynthesis, light reaction
c0031676cellular_componentplasma membrane-derived thylakoid membrane
c0046872molecular_functionmetal ion binding
d0005737cellular_componentcytoplasm
d0009523cellular_componentphotosystem II
d0009772biological_processphotosynthetic electron transport in photosystem II
d0010242molecular_functionoxygen evolving activity
d0015979biological_processphotosynthesis
d0016020cellular_componentmembrane
d0016168molecular_functionchlorophyll binding
d0016491molecular_functionoxidoreductase activity
d0019684biological_processphotosynthesis, light reaction
d0031676cellular_componentplasma membrane-derived thylakoid membrane
d0046872molecular_functionmetal ion binding
e0005506molecular_functioniron ion binding
e0005737cellular_componentcytoplasm
e0009055molecular_functionelectron transfer activity
e0009523cellular_componentphotosystem II
e0009539cellular_componentphotosystem II reaction center
e0009767biological_processphotosynthetic electron transport chain
e0015979biological_processphotosynthesis
e0016020cellular_componentmembrane
e0019684biological_processphotosynthesis, light reaction
e0020037molecular_functionheme binding
e0031676cellular_componentplasma membrane-derived thylakoid membrane
e0042651cellular_componentthylakoid membrane
e0046872molecular_functionmetal ion binding
f0005506molecular_functioniron ion binding
f0005737cellular_componentcytoplasm
f0009055molecular_functionelectron transfer activity
f0009523cellular_componentphotosystem II
f0009539cellular_componentphotosystem II reaction center
f0009767biological_processphotosynthetic electron transport chain
f0015979biological_processphotosynthesis
f0016020cellular_componentmembrane
f0019684biological_processphotosynthesis, light reaction
f0020037molecular_functionheme binding
f0031676cellular_componentplasma membrane-derived thylakoid membrane
f0042651cellular_componentthylakoid membrane
f0046872molecular_functionmetal ion binding
h0009523cellular_componentphotosystem II
h0015979biological_processphotosynthesis
h0016020cellular_componentmembrane
h0031676cellular_componentplasma membrane-derived thylakoid membrane
h0042301molecular_functionphosphate ion binding
h0050821biological_processprotein stabilization
i0005737cellular_componentcytoplasm
i0009523cellular_componentphotosystem II
i0009539cellular_componentphotosystem II reaction center
i0015979biological_processphotosynthesis
i0016020cellular_componentmembrane
i0031676cellular_componentplasma membrane-derived thylakoid membrane
i0042651cellular_componentthylakoid membrane
k0005737cellular_componentcytoplasm
k0009523cellular_componentphotosystem II
k0009539cellular_componentphotosystem II reaction center
k0015979biological_processphotosynthesis
k0031676cellular_componentplasma membrane-derived thylakoid membrane
k0042651cellular_componentthylakoid membrane
l0005737cellular_componentcytoplasm
l0009523cellular_componentphotosystem II
l0009539cellular_componentphotosystem II reaction center
l0015979biological_processphotosynthesis
l0016020cellular_componentmembrane
l0031676cellular_componentplasma membrane-derived thylakoid membrane
l0042651cellular_componentthylakoid membrane
m0005737cellular_componentcytoplasm
m0009523cellular_componentphotosystem II
m0015979biological_processphotosynthesis
m0016020cellular_componentmembrane
m0019684biological_processphotosynthesis, light reaction
m0031676cellular_componentplasma membrane-derived thylakoid membrane
m0042651cellular_componentthylakoid membrane
t0009523cellular_componentphotosystem II
t0009539cellular_componentphotosystem II reaction center
t0015979biological_processphotosynthesis
t0016020cellular_componentmembrane
t0031676cellular_componentplasma membrane-derived thylakoid membrane
t0042651cellular_componentthylakoid membrane
x0009523cellular_componentphotosystem II
x0015979biological_processphotosynthesis
x0016020cellular_componentmembrane
x0031676cellular_componentplasma membrane-derived thylakoid membrane
y0009523cellular_componentphotosystem II
y0015979biological_processphotosynthesis
y0016020cellular_componentmembrane
y0031676cellular_componentplasma membrane-derived thylakoid membrane
z0009523cellular_componentphotosystem II
z0009539cellular_componentphotosystem II reaction center
z0015979biological_processphotosynthesis
z0031676cellular_componentplasma membrane-derived thylakoid membrane
z0042549biological_processphotosystem II stabilization
z0042651cellular_componentthylakoid membrane
Functional Information from PROSITE/UniProt
site_idPS00244
Number of Residues27
DetailsREACTION_CENTER Photosynthetic reaction center proteins signature. NilmhPfHqlGvagvfggalfcAmHGS
ChainResidueDetails
aASN191-SER217
dASN190-ALA216

site_idPS00537
Number of Residues15
DetailsCYTOCHROME_B559 Cytochrome b559 subunits heme-binding site signature. ItSVRYwvIHSITIP
ChainResidueDetails
eILE14-PRO28
fILE15-PRO29

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues81
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues659
DetailsTopological domain: {"description":"Lumenal","evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues212
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12518057","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsSite: {"description":"Tyrosine radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12518057","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues1
DetailsSite: {"description":"Stabilizes free radical intermediate","evidences":[{"source":"HAMAP-Rule","id":"MF_01379","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues90
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01495","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues24
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues85
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues2
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_01383","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues14
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00642","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00642","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues16
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00643","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues1
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00643","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI27
Number of Residues138
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues1
DetailsModified residue: {"description":"Blocked amino end (Met)","evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"journal article","publicationDate":"1989","firstPage":"155","lastPage":"160","volume":"251","journal":"FEBS Lett.","title":"Identification of psbI and psbL gene products in cyanobacterial photosystem II reaction center preparation.","authors":["Ikeuchi M.","Koike H.","Inoue Y."],"citationCrossReferences":[{"database":"DOI","id":"10.1016/0014-5793(89)81446-2"}]}}]}
ChainResidueDetails

site_idSWS_FT_FI29
Number of Residues1
DetailsModified residue: {"description":"Blocked amino end (Met)","evidences":[{"source":"PubMed","id":"2503398","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI30
Number of Residues108
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_01496","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3WU2","evidenceCode":"ECO:0000312"}]}
ChainResidueDetails

site_idSWS_FT_FI31
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01496","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"21499260","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"23426624","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19433803","evidenceCode":"ECO:0000303"}]}
ChainResidueDetails

site_idSWS_FT_FI32
Number of Residues19
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"33846594","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7NHQ","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243911

PDB entries from 2025-10-29

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