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9KZ9

Cryo-EM structure of PSI-ACPI from Rhodomonas sp. NIES-2332 at 2.08 angstroms resolution

Functional Information from GO Data
ChainGOidnamespacecontents
A0000287molecular_functionmagnesium ion binding
A0009055molecular_functionelectron transfer activity
A0009535cellular_componentchloroplast thylakoid membrane
A0015979biological_processphotosynthesis
A0016020cellular_componentmembrane
B0000287molecular_functionmagnesium ion binding
B0009055molecular_functionelectron transfer activity
B0009535cellular_componentchloroplast thylakoid membrane
B0015979biological_processphotosynthesis
C0009055molecular_functionelectron transfer activity
C0009535cellular_componentchloroplast thylakoid membrane
C0015979biological_processphotosynthesis
D0009535cellular_componentchloroplast thylakoid membrane
D0009538cellular_componentphotosystem I reaction center
D0015979biological_processphotosynthesis
E0009535cellular_componentchloroplast thylakoid membrane
E0015979biological_processphotosynthesis
E0016020cellular_componentmembrane
I0009535cellular_componentchloroplast thylakoid membrane
I0015979biological_processphotosynthesis
I0055035cellular_componentplastid thylakoid membrane
J0009535cellular_componentchloroplast thylakoid membrane
J0015979biological_processphotosynthesis
K0009535cellular_componentchloroplast thylakoid membrane
K0015979biological_processphotosynthesis
K0016020cellular_componentmembrane
L0009535cellular_componentchloroplast thylakoid membrane
L0015979biological_processphotosynthesis
L0016020cellular_componentmembrane
M0009535cellular_componentchloroplast thylakoid membrane
M0015979biological_processphotosynthesis
Functional Information from PROSITE/UniProt
site_idPS00099
Number of Residues14
DetailsTHIOLASE_3 Thiolases active site. ALIAACVAsAsAfA
ChainResidueDetails
cALA6-ALA19

site_idPS00198
Number of Residues12
Details4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCTqCVrACP
ChainResidueDetails
CCYS11-PRO22
CCYS48-PRO59

site_idPS00419
Number of Residues10
DetailsPHOTOSYSTEM_I_PSAAB Photosystem I psaA and psaB proteins signature. CDGPGRGGTC
ChainResidueDetails
ACYS577-CYS586
BCYS558-CYS567

site_idPS01026
Number of Residues18
DetailsPHOTOSYSTEM_I_PSAGK Photosystem I psaG and psaK proteins signature. GFgLpEllAsTSlGHiVG
ChainResidueDetails
KGLY56-GLY73

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI11
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=I","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=II","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues24
DetailsTransmembrane: {"description":"Helical; Name=III","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=IV","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI15
Number of Residues23
DetailsTransmembrane: {"description":"Helical; Name=V","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI16
Number of Residues26
DetailsTransmembrane: {"description":"Helical; Name=VI","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI17
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=VII","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI18
Number of Residues18
DetailsTransmembrane: {"description":"Helical; Name=VIII","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI19
Number of Residues21
DetailsTransmembrane: {"description":"Helical; Name=IX","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI20
Number of Residues22
DetailsTransmembrane: {"description":"Helical; Name=X","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI21
Number of Residues20
DetailsTransmembrane: {"description":"Helical; Name=XI","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI22
Number of Residues4
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI23
Number of Residues2
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"HAMAP-Rule","id":"MF_00482","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI24
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"HAMAP-Rule","id":"MF_01303","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI25
Number of Residues29
DetailsDomain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"HAMAP-Rule","id":"MF_01303","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI26
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01303","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI28
Number of Residues20
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"HAMAP-Rule","id":"MF_00522","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

251174

PDB entries from 2026-03-25

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