3KDN
Crystal structure of Type III Rubisco SP4 mutant complexed with 2-CABP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0006196 | biological_process | AMP catabolic process |
| A | 0015977 | biological_process | carbon fixation |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0006196 | biological_process | AMP catabolic process |
| B | 0015977 | biological_process | carbon fixation |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0006196 | biological_process | AMP catabolic process |
| C | 0015977 | biological_process | carbon fixation |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0006196 | biological_process | AMP catabolic process |
| D | 0015977 | biological_process | carbon fixation |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016829 | molecular_function | lyase activity |
| D | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| D | 0046872 | molecular_function | metal ion binding |
| E | 0000287 | molecular_function | magnesium ion binding |
| E | 0006196 | biological_process | AMP catabolic process |
| E | 0015977 | biological_process | carbon fixation |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016829 | molecular_function | lyase activity |
| E | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0000287 | molecular_function | magnesium ion binding |
| F | 0006196 | biological_process | AMP catabolic process |
| F | 0015977 | biological_process | carbon fixation |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016829 | molecular_function | lyase activity |
| F | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0000287 | molecular_function | magnesium ion binding |
| G | 0006196 | biological_process | AMP catabolic process |
| G | 0015977 | biological_process | carbon fixation |
| G | 0016491 | molecular_function | oxidoreductase activity |
| G | 0016829 | molecular_function | lyase activity |
| G | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0000287 | molecular_function | magnesium ion binding |
| H | 0006196 | biological_process | AMP catabolic process |
| H | 0015977 | biological_process | carbon fixation |
| H | 0016491 | molecular_function | oxidoreductase activity |
| H | 0016829 | molecular_function | lyase activity |
| H | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| H | 0046872 | molecular_function | metal ion binding |
| I | 0000287 | molecular_function | magnesium ion binding |
| I | 0006196 | biological_process | AMP catabolic process |
| I | 0015977 | biological_process | carbon fixation |
| I | 0016491 | molecular_function | oxidoreductase activity |
| I | 0016829 | molecular_function | lyase activity |
| I | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| I | 0046872 | molecular_function | metal ion binding |
| J | 0000287 | molecular_function | magnesium ion binding |
| J | 0006196 | biological_process | AMP catabolic process |
| J | 0015977 | biological_process | carbon fixation |
| J | 0016491 | molecular_function | oxidoreductase activity |
| J | 0016829 | molecular_function | lyase activity |
| J | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
| J | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 500 |
| Chain | Residue |
| A | LYS165 |
| A | KCX189 |
| A | ASP191 |
| A | GLU192 |
| A | CAP600 |
| H | ASN111 |
| site_id | AC2 |
| Number of Residues | 26 |
| Details | BINDING SITE FOR RESIDUE CAP A 600 |
| Chain | Residue |
| A | KCX189 |
| A | ASP191 |
| A | GLU192 |
| A | HIS281 |
| A | ARG282 |
| A | HIS314 |
| A | LYS322 |
| A | LEU323 |
| A | SER367 |
| A | GLY368 |
| A | GLY369 |
| A | GLN389 |
| A | GLY391 |
| A | GLY392 |
| A | HOH495 |
| A | MG500 |
| A | HOH645 |
| A | HOH1278 |
| A | HOH1893 |
| A | HOH2850 |
| H | THR54 |
| H | TRP55 |
| H | ASN111 |
| A | VAL161 |
| A | LYS163 |
| A | LYS165 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG B 500 |
| Chain | Residue |
| B | KCX189 |
| B | ASP191 |
| B | GLU192 |
| B | CAP600 |
| site_id | AC4 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP B 600 |
| Chain | Residue |
| B | LYS163 |
| B | LYS165 |
| B | KCX189 |
| B | ASP191 |
| B | GLU192 |
| B | HIS281 |
| B | ARG282 |
| B | HIS314 |
| B | LYS322 |
| B | LEU323 |
| B | SER367 |
| B | GLY368 |
| B | GLY369 |
| B | GLN389 |
| B | GLY391 |
| B | GLY392 |
| B | HOH467 |
| B | HOH468 |
| B | HOH472 |
| B | HOH499 |
| B | MG500 |
| B | HOH2398 |
| B | HOH2720 |
| B | HOH2839 |
| G | GLU49 |
| G | TRP55 |
| G | ASN111 |
| G | HOH466 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 500 |
| Chain | Residue |
| C | KCX189 |
| C | ASP191 |
| C | GLU192 |
| C | CAP600 |
| F | ASN111 |
| site_id | AC6 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE CAP C 600 |
| Chain | Residue |
| C | LYS163 |
| C | LYS165 |
| C | KCX189 |
| C | ASP191 |
| C | GLU192 |
| C | HIS281 |
| C | ARG282 |
| C | HIS314 |
| C | LYS322 |
| C | LEU323 |
| C | SER367 |
| C | GLY368 |
| C | GLY369 |
| C | GLN389 |
| C | GLY391 |
| C | GLY392 |
| C | HOH445 |
| C | HOH457 |
| C | HOH461 |
| C | HOH487 |
| C | MG500 |
| C | HOH616 |
| C | HOH691 |
| C | HOH2321 |
| F | GLU49 |
| F | TRP55 |
| F | ASN111 |
| F | HOH503 |
| F | HOH1009 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 500 |
| Chain | Residue |
| D | ASP191 |
| D | GLU192 |
| D | CAP600 |
| D | KCX189 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP D 600 |
| Chain | Residue |
| D | LYS163 |
| D | LYS165 |
| D | KCX189 |
| D | ASP191 |
| D | GLU192 |
| D | HIS281 |
| D | ARG282 |
| D | HIS314 |
| D | LYS322 |
| D | LEU323 |
| D | SER367 |
| D | GLY368 |
| D | GLY369 |
| D | GLN389 |
| D | GLY391 |
| D | GLY392 |
| D | HOH445 |
| D | HOH452 |
| D | HOH458 |
| D | MG500 |
| D | HOH510 |
| D | HOH1721 |
| D | HOH2695 |
| D | HOH2855 |
| J | GLU49 |
| J | TRP55 |
| J | ASN111 |
| J | HOH2762 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 500 |
| Chain | Residue |
| E | KCX189 |
| E | ASP191 |
| E | GLU192 |
| E | CAP600 |
| site_id | BC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP E 600 |
| Chain | Residue |
| E | LYS163 |
| E | LYS165 |
| E | KCX189 |
| E | ASP191 |
| E | GLU192 |
| E | HIS281 |
| E | ARG282 |
| E | HIS314 |
| E | LYS322 |
| E | LEU323 |
| E | SER367 |
| E | GLY368 |
| E | GLY369 |
| E | GLN389 |
| E | GLY391 |
| E | GLY392 |
| E | HOH483 |
| E | HOH494 |
| E | MG500 |
| E | HOH654 |
| E | HOH676 |
| E | HOH1879 |
| E | HOH2240 |
| I | GLU49 |
| I | TRP55 |
| I | ASN111 |
| I | HOH463 |
| I | HOH465 |
| site_id | BC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG F 500 |
| Chain | Residue |
| C | ASN111 |
| F | KCX189 |
| F | ASP191 |
| F | GLU192 |
| F | CAP600 |
| site_id | BC3 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP F 600 |
| Chain | Residue |
| C | GLU49 |
| C | THR54 |
| C | TRP55 |
| C | ASN111 |
| C | HOH451 |
| C | HOH478 |
| F | LYS163 |
| F | LYS165 |
| F | KCX189 |
| F | ASP191 |
| F | GLU192 |
| F | HIS281 |
| F | ARG282 |
| F | HIS314 |
| F | LYS322 |
| F | LEU323 |
| F | SER367 |
| F | GLY368 |
| F | GLY369 |
| F | GLN389 |
| F | GLY391 |
| F | GLY392 |
| F | HOH445 |
| F | HOH464 |
| F | HOH490 |
| F | HOH495 |
| F | HOH498 |
| F | MG500 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG G 500 |
| Chain | Residue |
| B | ASN111 |
| G | KCX189 |
| G | ASP191 |
| G | GLU192 |
| G | CAP600 |
| site_id | BC5 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP G 600 |
| Chain | Residue |
| B | GLU49 |
| B | TRP55 |
| B | ASN111 |
| B | HOH448 |
| B | HOH454 |
| G | LYS163 |
| G | LYS165 |
| G | KCX189 |
| G | ASP191 |
| G | GLU192 |
| G | HIS281 |
| G | ARG282 |
| G | HIS314 |
| G | LYS322 |
| G | LEU323 |
| G | SER367 |
| G | GLY368 |
| G | GLY369 |
| G | GLN389 |
| G | GLY391 |
| G | GLY392 |
| G | HOH446 |
| G | HOH456 |
| G | HOH469 |
| G | HOH485 |
| G | MG500 |
| G | HOH530 |
| G | HOH1761 |
| site_id | BC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG H 500 |
| Chain | Residue |
| H | KCX189 |
| H | ASP191 |
| H | GLU192 |
| H | CAP600 |
| site_id | BC7 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE CAP H 600 |
| Chain | Residue |
| A | TRP55 |
| A | ASN111 |
| A | HOH1659 |
| H | LYS163 |
| H | LYS165 |
| H | KCX189 |
| H | ASP191 |
| H | GLU192 |
| H | HIS281 |
| H | ARG282 |
| H | HIS314 |
| H | LYS322 |
| H | LEU323 |
| H | SER367 |
| H | GLY368 |
| H | GLY369 |
| H | GLN389 |
| H | GLY391 |
| H | GLY392 |
| H | HOH457 |
| H | MG500 |
| H | HOH1169 |
| H | HOH1230 |
| H | HOH2657 |
| H | HOH2710 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG I 500 |
| Chain | Residue |
| I | KCX189 |
| I | ASP191 |
| I | GLU192 |
| I | CAP600 |
| site_id | BC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP I 600 |
| Chain | Residue |
| E | GLU49 |
| E | TRP55 |
| E | ASN111 |
| E | HOH505 |
| I | LYS163 |
| I | LYS165 |
| I | KCX189 |
| I | ASP191 |
| I | GLU192 |
| I | HIS281 |
| I | ARG282 |
| I | HIS314 |
| I | LYS322 |
| I | LEU323 |
| I | SER367 |
| I | GLY368 |
| I | GLY369 |
| I | GLN389 |
| I | GLY391 |
| I | GLY392 |
| I | HOH445 |
| I | HOH451 |
| I | HOH471 |
| I | HOH478 |
| I | HOH482 |
| I | HOH483 |
| I | HOH491 |
| I | MG500 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG J 500 |
| Chain | Residue |
| D | ASN111 |
| J | KCX189 |
| J | ASP191 |
| J | GLU192 |
| J | CAP600 |
| site_id | CC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP J 600 |
| Chain | Residue |
| D | GLU49 |
| D | TRP55 |
| D | ASN111 |
| D | HOH482 |
| D | HOH484 |
| J | LYS163 |
| J | LYS165 |
| J | KCX189 |
| J | ASP191 |
| J | GLU192 |
| J | HIS281 |
| J | ARG282 |
| J | HIS314 |
| J | LYS322 |
| J | LEU323 |
| J | SER367 |
| J | GLY368 |
| J | GLY369 |
| J | GLN389 |
| J | GLY391 |
| J | GLY392 |
| J | HOH445 |
| J | HOH481 |
| J | MG500 |
| J | HOH578 |
| J | HOH602 |
| J | HOH1892 |
| J | HOH1895 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"HAMAP-Rule","id":"MF_01133","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 80 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {"description":"via carbamate group","evidences":[{"source":"HAMAP-Rule","id":"MF_01133","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20926376","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01133","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20926376","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"source":"HAMAP-Rule","id":"MF_01133","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | Modified residue: {"description":"N6-carboxylysine","evidences":[{"source":"HAMAP-Rule","id":"MF_01133","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20926376","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |






