1WDD
Crystal Structure of Activated Rice Rubisco Complexed with 2-Carboxyarabinitol-1,5-bisphosphate
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004497 | molecular_function | monooxygenase activity |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009536 | cellular_component | plastid |
| A | 0009853 | biological_process | photorespiration |
| A | 0015977 | biological_process | carbon fixation |
| A | 0015979 | biological_process | photosynthesis |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| A | 0019253 | biological_process | reductive pentose-phosphate cycle |
| A | 0046872 | molecular_function | metal ion binding |
| E | 0000166 | molecular_function | nucleotide binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0004497 | molecular_function | monooxygenase activity |
| E | 0009507 | cellular_component | chloroplast |
| E | 0009536 | cellular_component | plastid |
| E | 0009853 | biological_process | photorespiration |
| E | 0015977 | biological_process | carbon fixation |
| E | 0015979 | biological_process | photosynthesis |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| E | 0019253 | biological_process | reductive pentose-phosphate cycle |
| E | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1476 |
| Chain | Residue |
| A | LYS177 |
| A | KCX201 |
| A | ASP203 |
| A | GLU204 |
| A | CAP1001 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG E 2476 |
| Chain | Residue |
| E | CAP2001 |
| E | LYS177 |
| E | KCX201 |
| E | ASP203 |
| E | GLU204 |
| site_id | AC3 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE CAP A 1001 |
| Chain | Residue |
| A | THR173 |
| A | LYS175 |
| A | LYS177 |
| A | KCX201 |
| A | ASP203 |
| A | GLU204 |
| A | HIS294 |
| A | ARG295 |
| A | HIS327 |
| A | LYS334 |
| A | LEU335 |
| A | SER379 |
| A | GLY380 |
| A | GLY381 |
| A | GLY403 |
| A | GLY404 |
| A | MG1476 |
| A | HOH3108 |
| A | HOH3109 |
| A | HOH3115 |
| A | HOH3117 |
| A | HOH3131 |
| A | HOH3132 |
| E | GLU60 |
| E | THR65 |
| E | TRP66 |
| E | ASN123 |
| E | HOH3028 |
| E | HOH3038 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE CAP E 2001 |
| Chain | Residue |
| A | GLU60 |
| A | THR65 |
| A | TRP66 |
| A | ASN123 |
| A | HOH3032 |
| A | HOH3055 |
| E | THR173 |
| E | LYS175 |
| E | LYS177 |
| E | KCX201 |
| E | ASP203 |
| E | GLU204 |
| E | HIS294 |
| E | ARG295 |
| E | HIS327 |
| E | LYS334 |
| E | LEU335 |
| E | SER379 |
| E | GLY380 |
| E | GLY381 |
| E | GLY403 |
| E | GLY404 |
| E | MG2476 |
| E | HOH3020 |
| E | HOH3044 |
| E | HOH3045 |
| E | HOH3046 |
| E | HOH3130 |
| E | HOH3131 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 3001 |
| Chain | Residue |
| A | LYS32 |
| A | PRO104 |
| A | LEU105 |
| A | ASP106 |
| A | HOH3027 |
| A | HOH3166 |
| A | HOH3167 |
| A | HOH3407 |
| E | HOH3142 |
| site_id | AC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL E 3002 |
| Chain | Residue |
| A | HOH3127 |
| A | HOH3204 |
| A | HOH3205 |
| E | LYS32 |
| E | PRO104 |
| E | LEU105 |
| E | ASP106 |
| E | HOH3053 |
| E | HOH3362 |
| E | HOH3375 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL E 3003 |
| Chain | Residue |
| A | LEU270 |
| E | LEU270 |
| E | MET297 |
| E | HOH3035 |
| E | HOH3036 |
| E | HOH3037 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 3004 |
| Chain | Residue |
| A | THR68 |
| A | GOL3010 |
| A | HOH3021 |
| A | HOH3036 |
| A | GLY16 |
| A | VAL17 |
| A | LYS18 |
| A | TYR20 |
| A | THR65 |
| A | THR67 |
| site_id | AC9 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL E 3005 |
| Chain | Residue |
| E | GLU52 |
| E | HOH3042 |
| E | HOH3058 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 3006 |
| Chain | Residue |
| A | GLU52 |
| A | HOH3029 |
| A | HOH3030 |
| A | HOH3259 |
| A | HOH3360 |
| site_id | BC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL W 3007 |
| Chain | Residue |
| E | ASN163 |
| E | ARG187 |
| W | GLU43 |
| W | ARG64 |
| W | TYR65 |
| W | TRP66 |
| W | ARG99 |
| W | GLN110 |
| W | HOH536 |
| W | HOH558 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL W 3008 |
| Chain | Residue |
| W | GLN2 |
| W | VAL3 |
| W | TRP69 |
| W | ALA92 |
| W | HOH312 |
| W | HOH669 |
| site_id | BC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL E 3009 |
| Chain | Residue |
| E | TYR226 |
| E | GLN229 |
| E | ALA230 |
| E | HOH3366 |
| W | VAL50 |
| W | ASN54 |
| W | ARG56 |
| W | HOH555 |
| site_id | BC5 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 3010 |
| Chain | Residue |
| A | LYS18 |
| A | THR23 |
| A | THR68 |
| A | ASP72 |
| A | LEU77 |
| A | GOL3004 |
| A | GOL3012 |
| A | HOH3038 |
| A | HOH3327 |
| site_id | BC6 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL E 3011 |
| Chain | Residue |
| E | GLY16 |
| E | VAL17 |
| E | LYS18 |
| E | TYR20 |
| E | THR65 |
| E | THR67 |
| E | THR68 |
| E | HOH3026 |
| E | HOH3049 |
| E | HOH3304 |
| site_id | BC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 3012 |
| Chain | Residue |
| A | VAL11 |
| A | PHE13 |
| A | THR68 |
| A | VAL69 |
| A | TRP70 |
| A | GLY73 |
| A | GOL3010 |
| W | PHE74 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL E 3013 |
| Chain | Residue |
| E | THR68 |
| E | VAL69 |
| E | TRP70 |
| E | HOH3183 |
| site_id | BC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL E 3014 |
| Chain | Residue |
| E | ARG295 |
| E | HIS298 |
| E | PHE311 |
| E | GLY329 |
| E | GLU336 |
| E | PHE345 |
| E | HOH3128 |
| E | HOH3133 |
| E | HOH3172 |
| E | HOH3300 |
| site_id | CC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE GOL A 3015 |
| Chain | Residue |
| A | ASN163 |
| A | ARG187 |
| A | HOH3303 |
| S | GLU43 |
| S | ARG64 |
| S | TYR65 |
| S | TRP66 |
| S | ARG99 |
| S | GLN110 |
| S | HOH177 |
| site_id | CC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL E 3016 |
| Chain | Residue |
| A | HOH3263 |
| E | ILE155 |
| E | GLN156 |
| E | ARG350 |
| E | ASP351 |
| E | ASP352 |
| E | PRO372 |
| E | GLY373 |
| E | HOH3141 |
| site_id | CC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 3017 |
| Chain | Residue |
| A | THR23 |
| A | LEU77 |
| A | ASP78 |
| A | LYS81 |
| A | HOH3161 |
Functional Information from PROSITE/UniProt
| site_id | PS00157 |
| Number of Residues | 9 |
| Details | RUBISCO_LARGE Ribulose bisphosphate carboxylase large chain active site. GlDFtKdDE |
| Chain | Residue | Details |
| A | GLY196-GLU204 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01338","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3AXK","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WDD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"in homodimeric partner","evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WDD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AXM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WDD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AXK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AXM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1WDD","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AXK","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3AXM","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PDB","id":"1WDD","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Site: {"description":"Transition state stabilizer"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"PubMed","id":"22609438","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI11 |
| Number of Residues | 8 |
| Details | Region: {"description":"Interaction with large subunit"} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| A | LYS175 | |
| A | HIS294 | |
| A | LYS177 | |
| A | ASP203 | |
| A | HIS327 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1rbl |
| Chain | Residue | Details |
| E | LYS175 | |
| E | HIS294 | |
| E | LYS177 | |
| E | ASP203 | |
| E | HIS327 |






