1MZ4
Crystal Structure of Cytochrome c550 from Thermosynechococcus elongatus
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005506 | molecular_function | iron ion binding |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009523 | cellular_component | photosystem II |
| A | 0015979 | biological_process | photosynthesis |
| A | 0019684 | biological_process | photosynthesis, light reaction |
| A | 0020037 | molecular_function | heme binding |
| A | 0022904 | biological_process | respiratory electron transport chain |
| A | 0031676 | cellular_component | plasma membrane-derived thylakoid membrane |
| A | 0042651 | cellular_component | thylakoid membrane |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE PO4 A 145 |
| Chain | Residue |
| A | THR4 |
| A | HOH185 |
| A | PRO5 |
| A | GLU6 |
| A | GLU23 |
| A | GLU87 |
| A | ILE88 |
| A | ALA89 |
| A | GLU90 |
| A | HOH167 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 146 |
| Chain | Residue |
| A | THR22 |
| A | GLU23 |
| A | LYS24 |
| A | GLU90 |
| A | HOH169 |
| A | HOH172 |
| A | HOH181 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE PO4 A 147 |
| Chain | Residue |
| A | TYR26 |
| A | LYS30 |
| A | ASP83 |
| A | GLU85 |
| A | GLN86 |
| A | GLU122 |
| A | LEU126 |
| A | PO4148 |
| A | HOH245 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 148 |
| Chain | Residue |
| A | HIS118 |
| A | GLU122 |
| A | LEU126 |
| A | PO4147 |
| A | HOH176 |
| A | HOH256 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 149 |
| Chain | Residue |
| A | LYS24 |
| A | GLU28 |
| A | HOH159 |
| A | HOH181 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BCT A 150 |
| Chain | Residue |
| A | LYS30 |
| A | LEU52 |
| A | THR81 |
| A | TYR82 |
| A | HEC151 |
| A | HOH162 |
| A | HOH208 |
| A | HOH248 |
| site_id | AC7 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE HEC A 151 |
| Chain | Residue |
| A | ALA36 |
| A | CYS37 |
| A | SER39 |
| A | CYS40 |
| A | HIS41 |
| A | THR46 |
| A | THR48 |
| A | LEU52 |
| A | ASP53 |
| A | LEU54 |
| A | THR58 |
| A | LEU59 |
| A | LEU72 |
| A | TYR75 |
| A | TYR82 |
| A | HIS92 |
| A | ILE115 |
| A | ILE119 |
| A | GOL141 |
| A | BCT150 |
| A | HOH153 |
| A | HOH154 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 140 |
| Chain | Residue |
| A | THR56 |
| A | ARG105 |
| A | HOH220 |
| A | HOH229 |
| A | HOH236 |
| A | HOH239 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 141 |
| Chain | Residue |
| A | LYS24 |
| A | GLU28 |
| A | ARG31 |
| A | THR48 |
| A | ASN49 |
| A | HEC151 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 142 |
| Chain | Residue |
| A | ASN13 |
| A | SER14 |
| A | GLY16 |
| A | ASP67 |
| A | ASN68 |
| A | ARG105 |
| A | HOH216 |
| site_id | BC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 143 |
| Chain | Residue |
| A | ARG31 |
| A | TYR35 |
| site_id | BC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 144 |
| Chain | Residue |
| A | GLU87 |
| A | ARG96 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"12881497","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16355230","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19219048","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14764885","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"20558739","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"21367867","evidenceCode":"ECO:0000303"},{"source":"PubMed","id":"25043005","evidenceCode":"ECO:0000303"},{"source":"Reference","evidenceCode":"ECO:0000303","citation":{"citationType":"journal article","publicationDate":"2004","firstPage":"4733","lastPage":"4736","volume":"6","journal":"Phys. Chem. Chem. Phys.","title":"Crystal structure of cyanobacterial photosystem II at 3.2 A resolution: a closer look at the Mn-cluster.","authors":["Biesiadka J.","Loll B.","Kern J.","Irrgangb K.-D.","Zouni A."],"citationCrossReferences":[{"database":"DOI","id":"10.1039/b406989g"}]}}]} |
| Chain | Residue | Details |






