3ITV
Crystal structure of Pseudomonas stutzeri L-rhamnose isomerase mutant S329K in complex with D-psicose
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0008740 | molecular_function | L-rhamnose isomerase activity |
A | 0016853 | molecular_function | isomerase activity |
A | 0019301 | biological_process | rhamnose catabolic process |
A | 0019324 | biological_process | L-lyxose metabolic process |
A | 0046872 | molecular_function | metal ion binding |
B | 0008740 | molecular_function | L-rhamnose isomerase activity |
B | 0016853 | molecular_function | isomerase activity |
B | 0019301 | biological_process | rhamnose catabolic process |
B | 0019324 | biological_process | L-lyxose metabolic process |
B | 0046872 | molecular_function | metal ion binding |
C | 0008740 | molecular_function | L-rhamnose isomerase activity |
C | 0016853 | molecular_function | isomerase activity |
C | 0019301 | biological_process | rhamnose catabolic process |
C | 0019324 | biological_process | L-lyxose metabolic process |
C | 0046872 | molecular_function | metal ion binding |
D | 0008740 | molecular_function | L-rhamnose isomerase activity |
D | 0016853 | molecular_function | isomerase activity |
D | 0019301 | biological_process | rhamnose catabolic process |
D | 0019324 | biological_process | L-lyxose metabolic process |
D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 501 |
Chain | Residue |
A | GLU219 |
A | ASP254 |
A | HIS281 |
A | ASP327 |
A | PSJ601 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN A 502 |
Chain | Residue |
A | HOH1994 |
A | HIS257 |
A | ASP289 |
A | PSJ601 |
A | HOH1639 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PSJ A 601 |
Chain | Residue |
A | TRP57 |
A | HIS101 |
A | TRP179 |
A | GLU219 |
A | LYS221 |
A | ASP254 |
A | HIS257 |
A | HIS281 |
A | ASP289 |
A | ASP327 |
A | LYS329 |
A | MN501 |
A | MN502 |
A | HOH563 |
A | HOH1994 |
B | PHE66 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 503 |
Chain | Residue |
B | GLU219 |
B | ASP254 |
B | HIS281 |
B | ASP327 |
B | PSJ602 |
site_id | AC5 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN B 504 |
Chain | Residue |
B | HIS257 |
B | ASP289 |
B | PSJ602 |
B | HOH1998 |
B | HOH1999 |
site_id | AC6 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE PSJ B 602 |
Chain | Residue |
A | PHE66 |
B | TRP57 |
B | HIS101 |
B | TRP179 |
B | GLU219 |
B | LYS221 |
B | ASP254 |
B | HIS257 |
B | HIS281 |
B | ASP289 |
B | ASP327 |
B | MN503 |
B | MN504 |
B | HOH552 |
B | HOH1999 |
site_id | AC7 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN C 505 |
Chain | Residue |
C | GLU219 |
C | ASP254 |
C | HIS281 |
C | ASP327 |
C | PSJ603 |
site_id | AC8 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN C 506 |
Chain | Residue |
C | HIS257 |
C | ASP289 |
C | PSJ603 |
C | HOH1273 |
C | HOH1996 |
site_id | AC9 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PSJ C 603 |
Chain | Residue |
C | TRP57 |
C | HIS101 |
C | TRP179 |
C | GLU219 |
C | LYS221 |
C | ASP254 |
C | HIS257 |
C | HIS281 |
C | ASP289 |
C | ASP327 |
C | ILE429 |
C | MN505 |
C | MN506 |
C | HOH573 |
C | HOH1273 |
D | PHE66 |
site_id | BC1 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN D 507 |
Chain | Residue |
D | GLU219 |
D | ASP254 |
D | HIS281 |
D | ASP327 |
D | PSJ604 |
site_id | BC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE MN D 508 |
Chain | Residue |
D | HIS257 |
D | ASP289 |
D | PSJ604 |
D | HOH1616 |
D | HOH1997 |
site_id | BC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE PSJ D 604 |
Chain | Residue |
D | MN507 |
D | MN508 |
D | HOH595 |
D | HOH1616 |
C | PHE66 |
D | TRP57 |
D | HIS101 |
D | TRP179 |
D | GLU219 |
D | LYS221 |
D | ASP254 |
D | HIS257 |
D | HIS281 |
D | ASP289 |
D | ASP327 |
D | LYS329 |