3A13
Crystal structure of Type III Rubisco SP4 mutant complexed with 2-CABP and activated with Ca
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 | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 445 |
| Chain | Residue |
| A | KCX189 |
| A | ASP191 |
| A | GLU192 |
| A | CAP446 |
| site_id | AC2 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE CAP A 446 |
| Chain | Residue |
| 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 | HOH508 |
| A | HOH523 |
| A | HOH528 |
| A | HOH529 |
| A | HOH535 |
| A | HOH554 |
| A | HOH584 |
| A | HOH625 |
| C | GLU49 |
| C | THR54 |
| C | TRP55 |
| C | ASN111 |
| A | LYS163 |
| A | LYS165 |
| A | KCX189 |
| A | ASP191 |
| A | GLU192 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE MG B 445 |
| Chain | Residue |
| B | ASN111 |
| B | LYS163 |
| B | LYS165 |
| B | KCX189 |
| B | ASP191 |
| B | GLU192 |
| B | CAP446 |
| site_id | AC4 |
| Number of Residues | 27 |
| 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 | HOH510 |
| B | HOH516 |
| B | HOH520 |
| B | HOH534 |
| B | HOH554 |
| B | HOH555 |
| B | HOH667 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG C 445 |
| Chain | Residue |
| C | LYS163 |
| C | KCX189 |
| C | ASP191 |
| C | GLU192 |
| C | CAP446 |
| site_id | AC6 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE CAP C 446 |
| Chain | Residue |
| A | GLU49 |
| A | TRP55 |
| A | ASN111 |
| C | LYS163 |
| C | LYS165 |
| C | KCX189 |
| 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 | HOH518 |
| C | HOH522 |
| C | HOH536 |
| C | HOH553 |
| C | HOH586 |
| C | HOH661 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG D 445 |
| Chain | Residue |
| D | GLU192 |
| D | CAP446 |
| D | KCX189 |
| D | ASP191 |
| site_id | AC8 |
| Number of Residues | 26 |
| 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 | SER367 |
| D | GLY368 |
| D | GLY369 |
| D | GLN389 |
| D | GLY391 |
| D | GLY392 |
| D | MG445 |
| D | HOH504 |
| D | HOH521 |
| D | HOH532 |
| D | HOH536 |
| D | HOH601 |
| D | HOH710 |
| E | GLU49 |
| E | THR54 |
| E | TRP55 |
| E | ASN111 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA E 445 |
| Chain | Residue |
| E | KCX189 |
| E | ASP191 |
| E | GLU192 |
| E | CAP446 |
| E | HOH666 |
| site_id | BC1 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE CAP E 446 |
| Chain | Residue |
| D | TRP55 |
| D | ASN111 |
| E | KCX189 |
| E | GLU192 |
| E | HIS281 |
| E | ARG282 |
| E | HIS314 |
| E | SER367 |
| E | GLY368 |
| E | GLY369 |
| E | GLN389 |
| E | LEU390 |
| E | GLY391 |
| E | GLY392 |
| E | CA445 |
| E | HOH528 |
| E | HOH535 |
| E | HOH556 |
| E | HOH577 |
| E | HOH627 |
| E | HOH666 |
| E | HOH687 |
| 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 | 28 |
| 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 | HOH520 |
| F | HOH524 |
| F | HOH528 |
| F | HOH541 |
| F | HOH562 |
| F | HOH570 |
| F | HOH623 |
| H | GLU49 |
| H | THR54 |
| H | TRP55 |
| H | ASN111 |
| site_id | BC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG G 445 |
| Chain | Residue |
| G | LYS163 |
| G | LYS165 |
| G | KCX189 |
| G | ASP191 |
| G | GLU192 |
| G | CAP446 |
| site_id | BC5 |
| Number of Residues | 27 |
| 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 | HOH503 |
| G | HOH528 |
| G | HOH536 |
| G | HOH582 |
| G | HOH603 |
| G | HOH669 |
| G | HOH672 |
| site_id | BC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG H 445 |
| Chain | Residue |
| H | LYS165 |
| H | KCX189 |
| H | ASP191 |
| H | GLU192 |
| H | CAP446 |
| site_id | BC7 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE CAP H 446 |
| Chain | Residue |
| F | TRP55 |
| F | ASN111 |
| F | HOH519 |
| H | LYS163 |
| H | LYS165 |
| H | KCX189 |
| 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 | HOH535 |
| H | HOH543 |
| H | HOH607 |
| H | HOH652 |
| site_id | BC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG I 445 |
| Chain | Residue |
| I | LYS163 |
| 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 | HOH536 |
| I | HOH537 |
| I | HOH543 |
| I | HOH547 |
| I | HOH575 |
| I | HOH659 |
| I | HOH673 |
| J | GLU49 |
| J | THR54 |
| J | TRP55 |
| J | ASN111 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA J 445 |
| Chain | Residue |
| J | KCX189 |
| J | ASP191 |
| J | GLU192 |
| J | CAP446 |
| J | HOH678 |
| site_id | CC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE CAP J 446 |
| Chain | Residue |
| I | TRP55 |
| I | ASN111 |
| J | KCX189 |
| J | GLU192 |
| J | HIS281 |
| J | ARG282 |
| J | HIS314 |
| J | SER367 |
| J | GLY368 |
| J | GLY369 |
| J | GLN389 |
| J | LEU390 |
| J | GLY391 |
| J | GLY392 |
| J | CA445 |
| J | HOH526 |
| J | HOH538 |
| J | HOH547 |
| J | HOH549 |
| J | HOH586 |
| J | HOH604 |
| J | HOH678 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 20 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|HAMAP-Rule:MF_01133 |
| Chain | Residue | Details |
| A | LYS163 | |
| E | HIS281 | |
| F | LYS163 | |
| F | HIS281 | |
| G | LYS163 | |
| G | HIS281 | |
| H | LYS163 | |
| H | HIS281 | |
| I | LYS163 | |
| I | HIS281 | |
| J | LYS163 | |
| A | HIS281 | |
| J | HIS281 | |
| B | LYS163 | |
| B | HIS281 | |
| C | LYS163 | |
| C | HIS281 | |
| D | LYS163 | |
| D | HIS281 | |
| E | LYS163 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 50 |
| Details | BINDING: BINDING => ECO:0000305 |
| Chain | Residue | Details |
| A | LYS165 | |
| B | GLN389 | |
| C | LYS165 | |
| C | ARG282 | |
| C | HIS314 | |
| C | SER367 | |
| C | GLN389 | |
| D | LYS165 | |
| D | ARG282 | |
| D | HIS314 | |
| D | SER367 | |
| A | ARG282 | |
| D | GLN389 | |
| E | LYS165 | |
| E | ARG282 | |
| E | HIS314 | |
| E | SER367 | |
| E | GLN389 | |
| F | LYS165 | |
| F | ARG282 | |
| F | HIS314 | |
| F | SER367 | |
| A | HIS314 | |
| F | GLN389 | |
| G | LYS165 | |
| G | ARG282 | |
| G | HIS314 | |
| G | SER367 | |
| G | GLN389 | |
| H | LYS165 | |
| H | ARG282 | |
| H | HIS314 | |
| H | SER367 | |
| A | SER367 | |
| H | GLN389 | |
| I | LYS165 | |
| I | ARG282 | |
| I | HIS314 | |
| I | SER367 | |
| I | GLN389 | |
| J | LYS165 | |
| J | ARG282 | |
| J | HIS314 | |
| J | SER367 | |
| A | GLN389 | |
| J | GLN389 | |
| B | LYS165 | |
| B | ARG282 | |
| B | HIS314 | |
| B | SER367 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | BINDING: via carbamate group => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 |
| Chain | Residue | Details |
| A | KCX189 | |
| J | KCX189 | |
| B | KCX189 | |
| C | KCX189 | |
| D | KCX189 | |
| E | KCX189 | |
| F | KCX189 | |
| G | KCX189 | |
| H | KCX189 | |
| I | KCX189 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 20 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 |
| Chain | Residue | Details |
| A | ASP191 | |
| E | GLU192 | |
| F | ASP191 | |
| F | GLU192 | |
| G | ASP191 | |
| G | GLU192 | |
| H | ASP191 | |
| H | GLU192 | |
| I | ASP191 | |
| I | GLU192 | |
| J | ASP191 | |
| A | GLU192 | |
| J | GLU192 | |
| B | ASP191 | |
| B | GLU192 | |
| C | ASP191 | |
| C | GLU192 | |
| D | ASP191 | |
| D | GLU192 | |
| E | ASP191 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | SITE: Transition state stabilizer => ECO:0000255|HAMAP-Rule:MF_01133 |
| Chain | Residue | Details |
| A | LYS322 | |
| J | LYS322 | |
| B | LYS322 | |
| C | LYS322 | |
| D | LYS322 | |
| E | LYS322 | |
| F | LYS322 | |
| G | LYS322 | |
| H | LYS322 | |
| I | LYS322 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 10 |
| Details | MOD_RES: N6-carboxylysine => ECO:0000255|HAMAP-Rule:MF_01133, ECO:0000269|PubMed:20926376 |
| Chain | Residue | Details |
| A | KCX189 | |
| J | KCX189 | |
| B | KCX189 | |
| C | KCX189 | |
| D | KCX189 | |
| E | KCX189 | |
| F | KCX189 | |
| G | KCX189 | |
| H | KCX189 | |
| I | KCX189 |
