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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9GC2

Cryo-EM structure of Arabidopsis thaliana PSI-LHCI- a603-NH mutant

Functional Information from GO Data
ChainGOidnamespacecontents
10009765biological_processphotosynthesis, light harvesting
10016020cellular_componentmembrane
20009765biological_processphotosynthesis, light harvesting
20016020cellular_componentmembrane
30009765biological_processphotosynthesis, light harvesting
30016020cellular_componentmembrane
40009765biological_processphotosynthesis, light harvesting
40016020cellular_componentmembrane
A0000287molecular_functionmagnesium ion binding
A0009055molecular_functionelectron transfer activity
A0009535cellular_componentchloroplast thylakoid membrane
A0009579cellular_componentthylakoid
A0015979biological_processphotosynthesis
A0016020cellular_componentmembrane
A0046872molecular_functionmetal ion binding
B0000287molecular_functionmagnesium ion binding
B0009055molecular_functionelectron transfer activity
B0009522cellular_componentphotosystem I
B0009535cellular_componentchloroplast thylakoid membrane
B0009579cellular_componentthylakoid
B0015979biological_processphotosynthesis
B0016020cellular_componentmembrane
C0003729molecular_functionmRNA binding
C0005634cellular_componentnucleus
C0009055molecular_functionelectron transfer activity
C0009507cellular_componentchloroplast
C0009522cellular_componentphotosystem I
C0009533cellular_componentchloroplast stromal thylakoid
C0009534cellular_componentchloroplast thylakoid
C0009535cellular_componentchloroplast thylakoid membrane
C0009536cellular_componentplastid
C0009773biological_processphotosynthetic electron transport in photosystem I
C0015979biological_processphotosynthesis
C0042651cellular_componentthylakoid membrane
C0051539molecular_function4 iron, 4 sulfur cluster binding
D0009522cellular_componentphotosystem I
D0009538cellular_componentphotosystem I reaction center
D0015979biological_processphotosynthesis
E0009522cellular_componentphotosystem I
E0009538cellular_componentphotosystem I reaction center
E0015979biological_processphotosynthesis
F0009522cellular_componentphotosystem I
F0009538cellular_componentphotosystem I reaction center
F0015979biological_processphotosynthesis
G0009522cellular_componentphotosystem I
G0009535cellular_componentchloroplast thylakoid membrane
G0015979biological_processphotosynthesis
G0016020cellular_componentmembrane
H0009522cellular_componentphotosystem I
H0009538cellular_componentphotosystem I reaction center
H0015979biological_processphotosynthesis
I0003674molecular_functionmolecular_function
I0009507cellular_componentchloroplast
I0009522cellular_componentphotosystem I
I0009535cellular_componentchloroplast thylakoid membrane
I0015979biological_processphotosynthesis
J0009522cellular_componentphotosystem I
J0009535cellular_componentchloroplast thylakoid membrane
J0009536cellular_componentplastid
J0015979biological_processphotosynthesis
K0009522cellular_componentphotosystem I
K0015979biological_processphotosynthesis
K0016020cellular_componentmembrane
L0009522cellular_componentphotosystem I
L0009538cellular_componentphotosystem I reaction center
L0015979biological_processphotosynthesis
N0009522cellular_componentphotosystem I
N0015979biological_processphotosynthesis
Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCTqCVrACP
ChainResidueDetails
CCYS11-PRO22
CCYS48-PRO59
site_idPS00228
Number of Residues4
DetailsTUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MRDL
ChainResidueDetails
JMET1-LEU4
site_idPS00419
Number of Residues10
DetailsPHOTOSYSTEM_I_PSAAB Photosystem I psaA and psaB proteins signature. CDGPGRGGTC
ChainResidueDetails
BCYS559-CYS568
ACYS573-CYS582
site_idPS01026
Number of Residues18
DetailsPHOTOSYSTEM_I_PSAGK Photosystem I psaG and psaK proteins signature. GFnIvDvlAwGSiGHiVA
ChainResidueDetails
GGLY126-ALA143
KGLY102-GLY119
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues356
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues17
DetailsBinding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues12
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues15
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P12333","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues13
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P07371","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22092075","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails
site_idSWS_FT_FI15
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"HAMAP-Rule","id":"MF_01303","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI16
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"HAMAP-Rule","id":"MF_01303","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI17
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01303","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI18
Number of Residues8
DetailsRegion: {"description":"Ferredoxin and ferredoxin-oxidoreductase binding","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI19
Number of Residues35
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

253795

PDB entries from 2026-05-20

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