2Z8S
Crystal structure of rhamnogalacturonan lyase YesW complexed with digalacturonic acid
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005576 | cellular_component | extracellular region |
A | 0016829 | molecular_function | lyase activity |
A | 0046872 | molecular_function | metal ion binding |
A | 0071555 | biological_process | cell wall organization |
A | 0102210 | molecular_function | rhamnogalacturonan endolyase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0016829 | molecular_function | lyase activity |
B | 0046872 | molecular_function | metal ion binding |
B | 0071555 | biological_process | cell wall organization |
B | 0102210 | molecular_function | rhamnogalacturonan endolyase activity |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 14 |
Details | BINDING: BINDING => ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2ZUX |
Chain | Residue | Details |
A | ASN152 | |
B | ASP187 | |
B | LYS207 | |
B | GLY238 | |
B | ARG255 | |
B | ASN532 | |
A | ASP172 | |
A | ASP187 | |
A | LYS207 | |
A | GLY238 | |
A | ARG255 | |
A | ASN532 | |
B | ASN152 | |
B | ASP172 |
site_id | SWS_FT_FI2 |
Number of Residues | 86 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17947240, ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8R, ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX |
Chain | Residue | Details |
A | ASP153 | |
A | LYS228 | |
A | GLU230 | |
A | HIS363 | |
A | ASP369 | |
A | ASP371 | |
A | ASP373 | |
A | LYS375 | |
A | GLU377 | |
A | ASP386 | |
A | HIS387 | |
A | ASP158 | |
A | HIS399 | |
A | ASP401 | |
A | ASP407 | |
A | ASP409 | |
A | ARG412 | |
A | GLY414 | |
A | GLU416 | |
A | GLU422 | |
A | ASP459 | |
A | TYR462 | |
A | ASP160 | |
A | GLY464 | |
A | GLU466 | |
A | ASP496 | |
A | ASP498 | |
A | LEU500 | |
A | GLU502 | |
A | ASP543 | |
A | LEU545 | |
A | ASP547 | |
A | ARG549 | |
A | ASP162 | |
A | GLU551 | |
A | ASN592 | |
A | ALA594 | |
A | ASN596 | |
B | ASP153 | |
B | ASP158 | |
B | ASP160 | |
B | ASP162 | |
B | GLN164 | |
B | GLU166 | |
A | GLN164 | |
B | ASP222 | |
B | ASP224 | |
B | ASP226 | |
B | LYS228 | |
B | GLU230 | |
B | HIS363 | |
B | ASP369 | |
B | ASP371 | |
B | ASP373 | |
B | LYS375 | |
A | GLU166 | |
B | GLU377 | |
B | ASP386 | |
B | HIS387 | |
B | HIS399 | |
B | ASP401 | |
B | ASP407 | |
B | ASP409 | |
B | ARG412 | |
B | GLY414 | |
B | GLU416 | |
A | ASP222 | |
B | GLU422 | |
B | ASP459 | |
B | TYR462 | |
B | GLY464 | |
B | GLU466 | |
B | ASP496 | |
B | ASP498 | |
B | LEU500 | |
B | GLU502 | |
B | ASP543 | |
A | ASP224 | |
B | LEU545 | |
B | ASP547 | |
B | ARG549 | |
B | GLU551 | |
B | ASN592 | |
B | ALA594 | |
B | ASN596 | |
A | ASP226 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | BINDING: BINDING => ECO:0000269|PubMed:17947240, ECO:0000269|PubMed:19193638, ECO:0007744|PDB:2Z8S, ECO:0007744|PDB:2ZUX |
Chain | Residue | Details |
A | ARG452 | |
A | ASP457 | |
A | TYR595 | |
B | ARG452 | |
B | ASP457 | |
B | TYR595 |