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7BW2

Crystal Structure of Cyanobacterial PSI Monomer from T.elongatus at 6.5 A Resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0005886cellular_componentplasma membrane
A0009055molecular_functionelectron transfer activity
A0009522cellular_componentphotosystem I
A0009579cellular_componentthylakoid
A0015979biological_processphotosynthesis
A0016020cellular_componentmembrane
A0016168molecular_functionchlorophyll binding
A0016491molecular_functionoxidoreductase activity
A0031676cellular_componentplasma membrane-derived thylakoid membrane
A0042651cellular_componentthylakoid membrane
A0046872molecular_functionmetal ion binding
A0051536molecular_functioniron-sulfur cluster binding
A0051539molecular_function4 iron, 4 sulfur cluster binding
B0000287molecular_functionmagnesium ion binding
B0005886cellular_componentplasma membrane
B0009055molecular_functionelectron transfer activity
B0009522cellular_componentphotosystem I
B0009579cellular_componentthylakoid
B0015979biological_processphotosynthesis
B0016020cellular_componentmembrane
B0016168molecular_functionchlorophyll binding
B0016491molecular_functionoxidoreductase activity
B0031676cellular_componentplasma membrane-derived thylakoid membrane
B0042651cellular_componentthylakoid membrane
B0046872molecular_functionmetal ion binding
B0051536molecular_functioniron-sulfur cluster binding
B0051539molecular_function4 iron, 4 sulfur cluster binding
C0009055molecular_functionelectron transfer activity
C0009522cellular_componentphotosystem I
C0009773biological_processphotosynthetic electron transport in photosystem I
C0015979biological_processphotosynthesis
C0016491molecular_functionoxidoreductase activity
C0031676cellular_componentplasma membrane-derived thylakoid membrane
C0042651cellular_componentthylakoid membrane
C0046872molecular_functionmetal ion binding
C0051536molecular_functioniron-sulfur cluster binding
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
E0031676cellular_componentplasma membrane-derived thylakoid membrane
E0042651cellular_componentthylakoid membrane
F0009522cellular_componentphotosystem I
F0009538cellular_componentphotosystem I reaction center
F0015979biological_processphotosynthesis
I0009522cellular_componentphotosystem I
I0015979biological_processphotosynthesis
I0031676cellular_componentplasma membrane-derived thylakoid membrane
I0042651cellular_componentthylakoid membrane
J0009522cellular_componentphotosystem I
J0015979biological_processphotosynthesis
J0031676cellular_componentplasma membrane-derived thylakoid membrane
J0042651cellular_componentthylakoid membrane
K0009522cellular_componentphotosystem I
K0015979biological_processphotosynthesis
K0016020cellular_componentmembrane
K0031676cellular_componentplasma membrane-derived thylakoid membrane
K0042651cellular_componentthylakoid membrane
L0009522cellular_componentphotosystem I
L0009538cellular_componentphotosystem I reaction center
L0015979biological_processphotosynthesis
L0031676cellular_componentplasma membrane-derived thylakoid membrane
L0042651cellular_componentthylakoid membrane
M0009522cellular_componentphotosystem I
M0015979biological_processphotosynthesis
M0031676cellular_componentplasma membrane-derived thylakoid membrane
M0042651cellular_componentthylakoid membrane
Functional Information from PROSITE/UniProt
site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCTqCVrACP
ChainResidueDetails
CCYS10-PRO21
CCYS47-PRO58

site_idPS00419
Number of Residues10
DetailsPHOTOSYSTEM_I_PSAAB Photosystem I psaA and psaB proteins signature. CDGPGRGGTC
ChainResidueDetails
ACYS578-CYS587
BCYS565-CYS574

site_idPS01026
Number of Residues18
DetailsPHOTOSYSTEM_I_PSAGK Photosystem I psaG and psaK proteins signature. GFgLpEllAtTSfGHlLA
ChainResidueDetails
KGLY53-ALA70

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues62
DetailsTransmembrane: {"description":"Helical; Name=I"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues504
DetailsTopological domain: {"description":"Lumenal, thylakoid","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues47
DetailsTransmembrane: {"description":"Helical; Name=II"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues314
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=III"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues34
DetailsTransmembrane: {"description":"Helical; Name=IV"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues46
DetailsTransmembrane: {"description":"Helical; Name=V"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues62
DetailsTransmembrane: {"description":"Helical; Name=VI"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues60
DetailsTransmembrane: {"description":"Helical; Name=VII"}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues49
DetailsTransmembrane: {"description":"Helical; Name=VIII"}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues59
DetailsTransmembrane: {"description":"Helical; Name=IX"}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues42
DetailsTransmembrane: {"description":"Helical; Name=X"}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues57
DetailsTransmembrane: {"description":"Helical; Name=XI"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"11418848","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues4
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"11418848","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"10066800","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"11418848","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 1"}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues31
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 2"}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues26
DetailsRegion: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues14
DetailsCompositional bias: {"description":"Polar residues","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues40
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues22
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00447","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues19
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00828","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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