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 | 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 |