9GBI
Cryo-EM structure of Arabidopsis thaliana PSI-LHCI wild-type
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009522 | cellular_component | photosystem I |
| A | 0009535 | cellular_component | chloroplast thylakoid membrane |
| A | 0015979 | biological_process | photosynthesis |
| A | 0016168 | molecular_function | chlorophyll binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0051536 | molecular_function | iron-sulfur cluster binding |
| A | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0009522 | cellular_component | photosystem I |
| B | 0009535 | cellular_component | chloroplast thylakoid membrane |
| B | 0015979 | biological_process | photosynthesis |
| B | 0016168 | molecular_function | chlorophyll binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0051536 | molecular_function | iron-sulfur cluster binding |
| B | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| C | 0003729 | molecular_function | mRNA binding |
| C | 0005634 | cellular_component | nucleus |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0009507 | cellular_component | chloroplast |
| C | 0009522 | cellular_component | photosystem I |
| C | 0009533 | cellular_component | chloroplast stromal thylakoid |
| C | 0009534 | cellular_component | chloroplast thylakoid |
| C | 0009535 | cellular_component | chloroplast thylakoid membrane |
| C | 0009536 | cellular_component | plastid |
| C | 0015979 | biological_process | photosynthesis |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0051536 | molecular_function | iron-sulfur cluster binding |
| C | 0051539 | molecular_function | 4 iron, 4 sulfur cluster binding |
| I | 0003674 | molecular_function | molecular_function |
| I | 0009507 | cellular_component | chloroplast |
| I | 0009522 | cellular_component | photosystem I |
| I | 0009535 | cellular_component | chloroplast thylakoid membrane |
| I | 0015979 | biological_process | photosynthesis |
| J | 0009522 | cellular_component | photosystem I |
| J | 0009535 | cellular_component | chloroplast thylakoid membrane |
| J | 0009536 | cellular_component | plastid |
| J | 0015979 | biological_process | photosynthesis |
Functional Information from PROSITE/UniProt
| site_id | PS00419 |
| Number of Residues | 10 |
| Details | PHOTOSYSTEM_I_PSAAB Photosystem I psaA and psaB proteins signature. CDGPGRGGTC |
| Chain | Residue | Details |
| B | CYS559-CYS568 | |
| A | CYS573-CYS582 |
| site_id | PS00228 |
| Number of Residues | 4 |
| Details | TUBULIN_B_AUTOREG Tubulin-beta mRNA autoregulation signal. MRDL |
| Chain | Residue | Details |
| J | MET1-LEU4 |
| site_id | PS00198 |
| Number of Residues | 12 |
| Details | 4FE4S_FER_1 4Fe-4S ferredoxin-type iron-sulfur binding region signature. CiGCTqCVrACP |
| Chain | Residue | Details |
| C | CYS11-PRO22 | |
| C | CYS48-PRO59 |
| site_id | PS01026 |
| Number of Residues | 18 |
| Details | PHOTOSYSTEM_I_PSAGK Photosystem I psaG and psaK proteins signature. GFtLaDtlAcGTvGHiIG |
| Chain | Residue | Details |
| K | GLY102-GLY119 | |
| G | GLY126-ALA143 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 356 |
| Details | Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 17 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 15 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"UniProtKB","id":"P12333","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 13 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P07371","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"22092075","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI12 |
| Number of Residues | 29 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 1","evidences":[{"source":"HAMAP-Rule","id":"MF_01303","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI13 |
| Number of Residues | 29 |
| Details | Domain: {"description":"4Fe-4S ferredoxin-type 2","evidences":[{"source":"HAMAP-Rule","id":"MF_01303","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI14 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01303","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI15 |
| Number of Residues | 8 |
| Details | Region: {"description":"Ferredoxin and ferredoxin-oxidoreductase binding","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI16 |
| Number of Residues | 35 |
| Details | Topological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
