1RSC
STRUCTURE OF AN EFFECTOR INDUCED INACTIVATED STATE OF RIBULOSE BISPHOSPHATE CARBOXYLASE(SLASH)OXYGENASE: THE BINARY COMPLEX BETWEEN ENZYME AND XYLULOSE BISPHOSPHATE
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000287 | molecular_function | magnesium ion binding |
A | 0004497 | molecular_function | monooxygenase activity |
A | 0005515 | molecular_function | protein binding |
A | 0009853 | biological_process | photorespiration |
A | 0015977 | biological_process | carbon fixation |
A | 0015979 | biological_process | photosynthesis |
A | 0016829 | molecular_function | lyase activity |
A | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
A | 0019253 | biological_process | reductive pentose-phosphate cycle |
A | 0031470 | cellular_component | carboxysome |
A | 0046872 | molecular_function | metal ion binding |
B | 0000287 | molecular_function | magnesium ion binding |
B | 0004497 | molecular_function | monooxygenase activity |
B | 0005515 | molecular_function | protein binding |
B | 0009853 | biological_process | photorespiration |
B | 0015977 | biological_process | carbon fixation |
B | 0015979 | biological_process | photosynthesis |
B | 0016829 | molecular_function | lyase activity |
B | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
B | 0019253 | biological_process | reductive pentose-phosphate cycle |
B | 0031470 | cellular_component | carboxysome |
B | 0046872 | molecular_function | metal ion binding |
C | 0000287 | molecular_function | magnesium ion binding |
C | 0004497 | molecular_function | monooxygenase activity |
C | 0005515 | molecular_function | protein binding |
C | 0009853 | biological_process | photorespiration |
C | 0015977 | biological_process | carbon fixation |
C | 0015979 | biological_process | photosynthesis |
C | 0016829 | molecular_function | lyase activity |
C | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
C | 0019253 | biological_process | reductive pentose-phosphate cycle |
C | 0031470 | cellular_component | carboxysome |
C | 0046872 | molecular_function | metal ion binding |
D | 0000287 | molecular_function | magnesium ion binding |
D | 0004497 | molecular_function | monooxygenase activity |
D | 0005515 | molecular_function | protein binding |
D | 0009853 | biological_process | photorespiration |
D | 0015977 | biological_process | carbon fixation |
D | 0015979 | biological_process | photosynthesis |
D | 0016829 | molecular_function | lyase activity |
D | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
D | 0019253 | biological_process | reductive pentose-phosphate cycle |
D | 0031470 | cellular_component | carboxysome |
D | 0046872 | molecular_function | metal ion binding |
E | 0000287 | molecular_function | magnesium ion binding |
E | 0004497 | molecular_function | monooxygenase activity |
E | 0005515 | molecular_function | protein binding |
E | 0009853 | biological_process | photorespiration |
E | 0015977 | biological_process | carbon fixation |
E | 0015979 | biological_process | photosynthesis |
E | 0016829 | molecular_function | lyase activity |
E | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
E | 0019253 | biological_process | reductive pentose-phosphate cycle |
E | 0031470 | cellular_component | carboxysome |
E | 0046872 | molecular_function | metal ion binding |
F | 0000287 | molecular_function | magnesium ion binding |
F | 0004497 | molecular_function | monooxygenase activity |
F | 0005515 | molecular_function | protein binding |
F | 0009853 | biological_process | photorespiration |
F | 0015977 | biological_process | carbon fixation |
F | 0015979 | biological_process | photosynthesis |
F | 0016829 | molecular_function | lyase activity |
F | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
F | 0019253 | biological_process | reductive pentose-phosphate cycle |
F | 0031470 | cellular_component | carboxysome |
F | 0046872 | molecular_function | metal ion binding |
G | 0000287 | molecular_function | magnesium ion binding |
G | 0004497 | molecular_function | monooxygenase activity |
G | 0005515 | molecular_function | protein binding |
G | 0009853 | biological_process | photorespiration |
G | 0015977 | biological_process | carbon fixation |
G | 0015979 | biological_process | photosynthesis |
G | 0016829 | molecular_function | lyase activity |
G | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
G | 0019253 | biological_process | reductive pentose-phosphate cycle |
G | 0031470 | cellular_component | carboxysome |
G | 0046872 | molecular_function | metal ion binding |
H | 0000287 | molecular_function | magnesium ion binding |
H | 0004497 | molecular_function | monooxygenase activity |
H | 0005515 | molecular_function | protein binding |
H | 0009853 | biological_process | photorespiration |
H | 0015977 | biological_process | carbon fixation |
H | 0015979 | biological_process | photosynthesis |
H | 0016829 | molecular_function | lyase activity |
H | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
H | 0019253 | biological_process | reductive pentose-phosphate cycle |
H | 0031470 | cellular_component | carboxysome |
H | 0046872 | molecular_function | metal ion binding |
I | 0009853 | biological_process | photorespiration |
I | 0015977 | biological_process | carbon fixation |
I | 0015979 | biological_process | photosynthesis |
I | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
I | 0019253 | biological_process | reductive pentose-phosphate cycle |
I | 0031470 | cellular_component | carboxysome |
J | 0009853 | biological_process | photorespiration |
J | 0015977 | biological_process | carbon fixation |
J | 0015979 | biological_process | photosynthesis |
J | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
J | 0019253 | biological_process | reductive pentose-phosphate cycle |
J | 0031470 | cellular_component | carboxysome |
K | 0009853 | biological_process | photorespiration |
K | 0015977 | biological_process | carbon fixation |
K | 0015979 | biological_process | photosynthesis |
K | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
K | 0019253 | biological_process | reductive pentose-phosphate cycle |
K | 0031470 | cellular_component | carboxysome |
L | 0009853 | biological_process | photorespiration |
L | 0015977 | biological_process | carbon fixation |
L | 0015979 | biological_process | photosynthesis |
L | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
L | 0019253 | biological_process | reductive pentose-phosphate cycle |
L | 0031470 | cellular_component | carboxysome |
M | 0009853 | biological_process | photorespiration |
M | 0015977 | biological_process | carbon fixation |
M | 0015979 | biological_process | photosynthesis |
M | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
M | 0019253 | biological_process | reductive pentose-phosphate cycle |
M | 0031470 | cellular_component | carboxysome |
N | 0009853 | biological_process | photorespiration |
N | 0015977 | biological_process | carbon fixation |
N | 0015979 | biological_process | photosynthesis |
N | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
N | 0019253 | biological_process | reductive pentose-phosphate cycle |
N | 0031470 | cellular_component | carboxysome |
O | 0009853 | biological_process | photorespiration |
O | 0015977 | biological_process | carbon fixation |
O | 0015979 | biological_process | photosynthesis |
O | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
O | 0019253 | biological_process | reductive pentose-phosphate cycle |
O | 0031470 | cellular_component | carboxysome |
P | 0009853 | biological_process | photorespiration |
P | 0015977 | biological_process | carbon fixation |
P | 0015979 | biological_process | photosynthesis |
P | 0016984 | molecular_function | ribulose-bisphosphate carboxylase activity |
P | 0019253 | biological_process | reductive pentose-phosphate cycle |
P | 0031470 | cellular_component | carboxysome |
Functional Information from PDB Data
site_id | 1P |
Number of Residues | 4 |
Details |
Chain | Residue |
A | LYS334 |
A | GLY381 |
A | GLY403 |
A | GLY404 |
site_id | 1P2 |
Number of Residues | 4 |
Details |
Chain | Residue |
B | LYS334 |
B | GLY381 |
B | GLY403 |
B | GLY404 |
site_id | 1P3 |
Number of Residues | 4 |
Details |
Chain | Residue |
C | LYS334 |
C | GLY381 |
C | GLY403 |
C | GLY404 |
site_id | 1P4 |
Number of Residues | 4 |
Details |
Chain | Residue |
D | LYS334 |
D | GLY381 |
D | GLY403 |
D | GLY404 |
site_id | 1P5 |
Number of Residues | 4 |
Details |
Chain | Residue |
E | LYS334 |
E | GLY381 |
E | GLY403 |
E | GLY404 |
site_id | 1P6 |
Number of Residues | 4 |
Details |
Chain | Residue |
F | LYS334 |
F | GLY381 |
F | GLY403 |
F | GLY404 |
site_id | 1P7 |
Number of Residues | 4 |
Details |
Chain | Residue |
G | LYS334 |
G | GLY381 |
G | GLY403 |
G | GLY404 |
site_id | 1P8 |
Number of Residues | 4 |
Details |
Chain | Residue |
H | LYS334 |
H | GLY381 |
H | GLY403 |
H | GLY404 |
site_id | 2P |
Number of Residues | 3 |
Details |
Chain | Residue |
A | HIS327 |
A | ARG295 |
A | SER379 |
site_id | 2P2 |
Number of Residues | 3 |
Details |
Chain | Residue |
B | HIS327 |
B | ARG295 |
B | SER379 |
site_id | 2P3 |
Number of Residues | 3 |
Details |
Chain | Residue |
C | HIS327 |
C | ARG295 |
C | SER379 |
site_id | 2P4 |
Number of Residues | 3 |
Details |
Chain | Residue |
D | HIS327 |
D | ARG295 |
D | SER379 |
site_id | 2P6 |
Number of Residues | 3 |
Details |
Chain | Residue |
F | HIS327 |
F | ARG295 |
F | SER379 |
site_id | 2P7 |
Number of Residues | 3 |
Details |
Chain | Residue |
G | HIS327 |
G | ARG295 |
G | SER379 |
site_id | 3P5 |
Number of Residues | 3 |
Details |
Chain | Residue |
E | HIS327 |
E | ARG295 |
E | SER379 |
site_id | 3P8 |
Number of Residues | 3 |
Details |
Chain | Residue |
H | HIS327 |
H | ARG295 |
H | SER379 |
site_id | AC1 |
Number of Residues | 25 |
Details | BINDING SITE FOR RESIDUE XBP A 476 |
Chain | Residue |
A | LYS175 |
A | LYS177 |
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 | HOH496 |
A | HOH588 |
A | HOH589 |
A | HOH590 |
A | HOH598 |
A | HOH599 |
B | GLU60 |
B | THR65 |
B | TRP66 |
B | ASN123 |
B | HOH477 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE XBP B 476 |
Chain | Residue |
A | GLU60 |
A | THR65 |
A | TRP66 |
A | ASN123 |
A | HOH615 |
B | LYS175 |
B | LYS177 |
B | ASP203 |
B | GLU204 |
B | HIS294 |
B | ARG295 |
B | HIS327 |
B | LYS334 |
B | LEU335 |
B | SER379 |
B | GLY380 |
B | GLY381 |
B | GLY403 |
B | GLY404 |
B | HOH479 |
site_id | AC3 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE XBP C 476 |
Chain | Residue |
C | LYS175 |
C | LYS177 |
C | ASP203 |
C | GLU204 |
C | HIS294 |
C | ARG295 |
C | HIS327 |
C | LYS334 |
C | LEU335 |
C | SER379 |
C | GLY380 |
C | GLY381 |
C | GLY403 |
C | GLY404 |
D | GLU60 |
D | THR65 |
D | TRP66 |
D | ASN123 |
site_id | AC4 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE XBP D 476 |
Chain | Residue |
C | GLU60 |
C | THR65 |
C | TRP66 |
C | ASN123 |
D | LYS175 |
D | LYS177 |
D | ASP203 |
D | GLU204 |
D | HIS294 |
D | ARG295 |
D | HIS327 |
D | LYS334 |
D | LEU335 |
D | SER379 |
D | GLY380 |
D | GLY381 |
D | GLY403 |
D | GLY404 |
site_id | AC5 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE XBP E 476 |
Chain | Residue |
E | LYS175 |
E | LYS177 |
E | ASP203 |
E | GLU204 |
E | HIS294 |
E | ARG295 |
E | HIS327 |
E | LYS334 |
E | LEU335 |
E | SER379 |
E | GLY380 |
E | GLY381 |
E | GLY403 |
E | GLY404 |
F | GLU60 |
F | THR65 |
F | TRP66 |
F | ASN123 |
site_id | AC6 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE XBP F 476 |
Chain | Residue |
E | GLU60 |
E | THR65 |
E | TRP66 |
E | ASN123 |
F | LYS175 |
F | LYS177 |
F | ASP203 |
F | GLU204 |
F | HIS294 |
F | ARG295 |
F | HIS327 |
F | LYS334 |
F | LEU335 |
F | SER379 |
F | GLY380 |
F | GLY381 |
F | GLY403 |
F | GLY404 |
site_id | AC7 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE XBP G 476 |
Chain | Residue |
G | LYS175 |
G | LYS177 |
G | ASP203 |
G | GLU204 |
G | HIS294 |
G | ARG295 |
G | HIS327 |
G | LYS334 |
G | LEU335 |
G | SER379 |
G | GLY380 |
G | GLY381 |
G | GLY403 |
G | GLY404 |
H | GLU60 |
H | THR65 |
H | TRP66 |
H | ASN123 |
site_id | AC8 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE XBP H 476 |
Chain | Residue |
G | GLU60 |
G | THR65 |
G | TRP66 |
G | ASN123 |
H | LYS175 |
H | LYS177 |
H | ASP203 |
H | GLU204 |
H | HIS294 |
H | ARG295 |
H | HIS327 |
H | LYS334 |
H | LEU335 |
H | SER379 |
H | GLY380 |
H | GLY381 |
H | GLY403 |
H | GLY404 |
site_id | BP2 |
Number of Residues | 6 |
Details |
Chain | Residue |
B | LYS175 |
B | ASP203 |
B | GLU204 |
B | HIS294 |
B | LYS334 |
B | SER379 |
site_id | BP3 |
Number of Residues | 6 |
Details |
Chain | Residue |
C | LYS175 |
C | ASP203 |
C | GLU204 |
C | HIS294 |
C | LYS334 |
C | SER379 |
site_id | BP4 |
Number of Residues | 6 |
Details |
Chain | Residue |
D | LYS175 |
D | ASP203 |
D | GLU204 |
D | HIS294 |
D | LYS334 |
D | SER379 |
site_id | BP5 |
Number of Residues | 6 |
Details |
Chain | Residue |
E | LYS175 |
E | ASP203 |
E | GLU204 |
E | HIS294 |
E | LYS334 |
E | SER379 |
site_id | BP6 |
Number of Residues | 6 |
Details |
Chain | Residue |
F | LYS175 |
F | ASP203 |
F | GLU204 |
F | HIS294 |
F | LYS334 |
F | SER379 |
site_id | BP7 |
Number of Residues | 6 |
Details |
Chain | Residue |
G | LYS175 |
G | ASP203 |
G | GLU204 |
G | HIS294 |
G | LYS334 |
G | SER379 |
site_id | BP8 |
Number of Residues | 6 |
Details |
Chain | Residue |
H | ASP203 |
H | GLU204 |
H | HIS294 |
H | LYS334 |
H | SER379 |
H | LYS175 |
site_id | XBP |
Number of Residues | 6 |
Details |
Chain | Residue |
A | GLU204 |
A | HIS294 |
A | LYS334 |
A | SER379 |
A | LYS175 |
A | ASP203 |
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 | 16 |
Details | ACT_SITE: Proton acceptor |
Chain | Residue | Details |
A | LYS175 | |
E | HIS294 | |
F | LYS175 | |
F | HIS294 | |
G | LYS175 | |
G | HIS294 | |
H | LYS175 | |
H | HIS294 | |
A | HIS294 | |
B | LYS175 | |
B | HIS294 | |
C | LYS175 | |
C | HIS294 | |
D | LYS175 | |
D | HIS294 | |
E | LYS175 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: in homodimeric partner |
Chain | Residue | Details |
A | ASN123 | |
B | ASN123 | |
C | ASN123 | |
D | ASN123 | |
E | ASN123 | |
F | ASN123 | |
G | ASN123 | |
H | ASN123 |
site_id | SWS_FT_FI3 |
Number of Residues | 40 |
Details | BINDING: |
Chain | Residue | Details |
A | THR173 | |
B | SER379 | |
C | THR173 | |
C | LYS177 | |
C | ARG295 | |
C | HIS327 | |
C | SER379 | |
D | THR173 | |
D | LYS177 | |
D | ARG295 | |
D | HIS327 | |
A | LYS177 | |
D | SER379 | |
E | THR173 | |
E | LYS177 | |
E | ARG295 | |
E | HIS327 | |
E | SER379 | |
F | THR173 | |
F | LYS177 | |
F | ARG295 | |
F | HIS327 | |
A | ARG295 | |
F | SER379 | |
G | THR173 | |
G | LYS177 | |
G | ARG295 | |
G | HIS327 | |
G | SER379 | |
H | THR173 | |
H | LYS177 | |
H | ARG295 | |
H | HIS327 | |
A | HIS327 | |
H | SER379 | |
A | SER379 | |
B | THR173 | |
B | LYS177 | |
B | ARG295 | |
B | HIS327 |
site_id | SWS_FT_FI4 |
Number of Residues | 8 |
Details | BINDING: via carbamate group => ECO:0000269|PubMed:8245022 |
Chain | Residue | Details |
A | LYS201 | |
B | LYS201 | |
C | LYS201 | |
D | LYS201 | |
E | LYS201 | |
F | LYS201 | |
G | LYS201 | |
H | LYS201 |
site_id | SWS_FT_FI5 |
Number of Residues | 16 |
Details | BINDING: BINDING => ECO:0000269|PubMed:8245022 |
Chain | Residue | Details |
A | ASP203 | |
E | GLU204 | |
F | ASP203 | |
F | GLU204 | |
G | ASP203 | |
G | GLU204 | |
H | ASP203 | |
H | GLU204 | |
A | GLU204 | |
B | ASP203 | |
B | GLU204 | |
C | ASP203 | |
C | GLU204 | |
D | ASP203 | |
D | GLU204 | |
E | ASP203 |
site_id | SWS_FT_FI6 |
Number of Residues | 8 |
Details | SITE: Transition state stabilizer |
Chain | Residue | Details |
A | LYS334 | |
B | LYS334 | |
C | LYS334 | |
D | LYS334 | |
E | LYS334 | |
F | LYS334 | |
G | LYS334 | |
H | LYS334 |
site_id | SWS_FT_FI7 |
Number of Residues | 8 |
Details | MOD_RES: N6-carboxylysine => ECO:0000269|PubMed:16593333 |
Chain | Residue | Details |
A | LYS201 | |
B | LYS201 | |
C | LYS201 | |
D | LYS201 | |
E | LYS201 | |
F | LYS201 | |
G | LYS201 | |
H | LYS201 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1rbl |
Chain | Residue | Details |
A | LYS175 | |
A | LYS201 | |
A | LYS177 | |
A | HIS294 | |
A | ASP203 | |
A | HIS327 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1rbl |
Chain | Residue | Details |
B | LYS175 | |
B | LYS201 | |
B | LYS177 | |
B | HIS294 | |
B | ASP203 | |
B | HIS327 |
site_id | CSA3 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1rbl |
Chain | Residue | Details |
C | LYS175 | |
C | LYS201 | |
C | LYS177 | |
C | HIS294 | |
C | ASP203 | |
C | HIS327 |
site_id | CSA4 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1rbl |
Chain | Residue | Details |
D | LYS175 | |
D | LYS201 | |
D | LYS177 | |
D | HIS294 | |
D | ASP203 | |
D | HIS327 |
site_id | CSA5 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1rbl |
Chain | Residue | Details |
E | LYS175 | |
E | LYS201 | |
E | LYS177 | |
E | HIS294 | |
E | ASP203 | |
E | HIS327 |
site_id | CSA6 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1rbl |
Chain | Residue | Details |
F | LYS175 | |
F | LYS201 | |
F | LYS177 | |
F | HIS294 | |
F | ASP203 | |
F | HIS327 |
site_id | CSA7 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1rbl |
Chain | Residue | Details |
G | LYS175 | |
G | LYS201 | |
G | LYS177 | |
G | HIS294 | |
G | ASP203 | |
G | HIS327 |
site_id | CSA8 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1rbl |
Chain | Residue | Details |
H | LYS175 | |
H | LYS201 | |
H | LYS177 | |
H | HIS294 | |
H | ASP203 | |
H | HIS327 |
site_id | MCSA1 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
A | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
A | LYS201 | metal ligand, nucleophile, proton donor |
A | ASP203 | metal ligand |
A | GLU204 | metal ligand |
A | HIS294 | proton acceptor |
A | LYS334 | electrostatic stabiliser |
site_id | MCSA2 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
B | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
B | LYS201 | metal ligand, nucleophile, proton donor |
B | ASP203 | metal ligand |
B | GLU204 | metal ligand |
B | HIS294 | proton acceptor |
B | LYS334 | electrostatic stabiliser |
site_id | MCSA3 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
C | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
C | LYS201 | metal ligand, nucleophile, proton donor |
C | ASP203 | metal ligand |
C | GLU204 | metal ligand |
C | HIS294 | proton acceptor |
C | LYS334 | electrostatic stabiliser |
site_id | MCSA4 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
D | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
D | LYS201 | metal ligand, nucleophile, proton donor |
D | ASP203 | metal ligand |
D | GLU204 | metal ligand |
D | HIS294 | proton acceptor |
D | LYS334 | electrostatic stabiliser |
site_id | MCSA5 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
E | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
E | LYS201 | metal ligand, nucleophile, proton donor |
E | ASP203 | metal ligand |
E | GLU204 | metal ligand |
E | HIS294 | proton acceptor |
E | LYS334 | electrostatic stabiliser |
site_id | MCSA6 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
F | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
F | LYS201 | metal ligand, nucleophile, proton donor |
F | ASP203 | metal ligand |
F | GLU204 | metal ligand |
F | HIS294 | proton acceptor |
F | LYS334 | electrostatic stabiliser |
site_id | MCSA7 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
G | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
G | LYS201 | metal ligand, nucleophile, proton donor |
G | ASP203 | metal ligand |
G | GLU204 | metal ligand |
G | HIS294 | proton acceptor |
G | LYS334 | electrostatic stabiliser |
site_id | MCSA8 |
Number of Residues | 6 |
Details | M-CSA 907 |
Chain | Residue | Details |
H | LYS175 | electrostatic stabiliser, metal ligand, proton donor |
H | LYS201 | metal ligand, nucleophile, proton donor |
H | ASP203 | metal ligand |
H | GLU204 | metal ligand |
H | HIS294 | proton acceptor |
H | LYS334 | electrostatic stabiliser |