3A12
Crystal structure of Type III Rubisco 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 | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 445 |
| Chain | Residue |
| A | KCX189 |
| A | ASP191 |
| A | GLU192 |
| A | CAP446 |
| C | ASN111 |
| site_id | AC2 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE CAP A 446 |
| Chain | Residue |
| 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 | MG445 |
| A | HOH521 |
| A | HOH523 |
| A | HOH528 |
| A | HOH574 |
| A | HOH579 |
| A | HOH615 |
| A | HOH626 |
| A | HOH684 |
| C | GLU49 |
| C | THR54 |
| C | TRP55 |
| C | ASN111 |
| A | VAL161 |
| A | LYS163 |
| A | LYS165 |
| A | KCX189 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 445 |
| Chain | Residue |
| B | ASN111 |
| B | KCX189 |
| B | ASP191 |
| B | GLU192 |
| B | CAP446 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE CAP B 446 |
| Chain | Residue |
| B | GLU49 |
| B | TRP55 |
| B | ASN111 |
| 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 | MG445 |
| B | HOH519 |
| B | HOH521 |
| B | HOH542 |
| B | HOH551 |
| B | HOH556 |
| B | HOH559 |
| B | HOH692 |
| B | HOH712 |
| B | HOH713 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG C 445 |
| Chain | Residue |
| C | KCX189 |
| C | ASP191 |
| C | GLU192 |
| C | CAP446 |
| site_id | AC6 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP C 446 |
| Chain | Residue |
| C | HOH658 |
| C | HOH740 |
| A | GLU49 |
| A | TRP55 |
| A | ASN111 |
| A | HOH611 |
| 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 | MG445 |
| C | HOH524 |
| C | HOH528 |
| C | HOH557 |
| C | HOH562 |
| C | HOH591 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 445 |
| Chain | Residue |
| D | KCX189 |
| D | ASP191 |
| D | GLU192 |
| D | CAP446 |
| site_id | AC8 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP D 446 |
| 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 | MG445 |
| D | HOH515 |
| D | HOH519 |
| D | HOH524 |
| D | HOH537 |
| D | HOH538 |
| D | HOH539 |
| D | HOH665 |
| D | HOH716 |
| E | GLU49 |
| E | TRP55 |
| E | ASN111 |
| site_id | AC9 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG E 445 |
| Chain | Residue |
| E | KCX189 |
| E | ASP191 |
| E | GLU192 |
| E | CAP446 |
| site_id | BC1 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP E 446 |
| Chain | Residue |
| D | GLU49 |
| D | TRP55 |
| D | ASN111 |
| D | HOH682 |
| 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 | MG445 |
| E | HOH525 |
| E | HOH532 |
| E | HOH543 |
| E | HOH570 |
| E | HOH574 |
| E | HOH580 |
| E | HOH608 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG F 445 |
| Chain | Residue |
| F | KCX189 |
| F | ASP191 |
| F | GLU192 |
| F | CAP446 |
| site_id | BC3 |
| Number of Residues | 27 |
| Details | BINDING SITE FOR RESIDUE CAP F 446 |
| Chain | Residue |
| 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 | MG445 |
| F | HOH519 |
| F | HOH525 |
| F | HOH536 |
| F | HOH537 |
| F | HOH556 |
| H | GLU49 |
| H | THR54 |
| H | TRP55 |
| H | ASN111 |
| H | HOH513 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG G 445 |
| Chain | Residue |
| G | KCX189 |
| G | ASP191 |
| G | GLU192 |
| G | CAP446 |
| site_id | BC5 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE CAP G 446 |
| Chain | Residue |
| G | GLU49 |
| G | TRP55 |
| G | ASN111 |
| 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 | MG445 |
| G | HOH507 |
| G | HOH524 |
| G | HOH529 |
| G | HOH536 |
| G | HOH540 |
| G | HOH561 |
| G | HOH574 |
| G | HOH602 |
| G | HOH607 |
| site_id | BC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG H 445 |
| Chain | Residue |
| F | ASN111 |
| H | LYS163 |
| H | LYS165 |
| H | KCX189 |
| H | ASP191 |
| H | GLU192 |
| H | CAP446 |
| site_id | BC7 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP H 446 |
| Chain | Residue |
| F | GLU49 |
| F | TRP55 |
| F | ASN111 |
| 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 | MG445 |
| H | HOH520 |
| H | HOH547 |
| H | HOH571 |
| H | HOH584 |
| H | HOH595 |
| H | HOH601 |
| H | HOH604 |
| H | HOH613 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG I 445 |
| Chain | Residue |
| I | KCX189 |
| I | ASP191 |
| I | GLU192 |
| I | CAP446 |
| site_id | BC9 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP I 446 |
| Chain | Residue |
| 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 | MG445 |
| I | HOH515 |
| I | HOH518 |
| I | HOH521 |
| I | HOH525 |
| I | HOH531 |
| I | HOH616 |
| I | HOH662 |
| I | HOH744 |
| J | GLU49 |
| J | TRP55 |
| J | ASN111 |
| site_id | CC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG J 445 |
| Chain | Residue |
| I | ASN111 |
| J | LYS163 |
| J | KCX189 |
| J | ASP191 |
| J | GLU192 |
| J | CAP446 |
| site_id | CC2 |
| Number of Residues | 28 |
| Details | BINDING SITE FOR RESIDUE CAP J 446 |
| Chain | Residue |
| I | GLU49 |
| I | TRP55 |
| I | ASN111 |
| I | HOH603 |
| 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 | MG445 |
| J | HOH502 |
| J | HOH546 |
| J | HOH566 |
| J | HOH580 |
| J | HOH586 |
| J | HOH587 |
| J | HOH633 |
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 |






