4OK4
Crystal Structure of Alg17c Mutant H202L
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 800 |
| Chain | Residue |
| A | HIS415 |
| A | ASP433 |
| A | HIS464 |
| A | HOH914 |
| A | HOH1238 |
| A | HOH1590 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 800 |
| Chain | Residue |
| B | HOH903 |
| B | HOH910 |
| B | HOH914 |
| B | HIS415 |
| B | ASP433 |
| B | HIS464 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:24478312 |
| Chain | Residue | Details |
| A | TYR258 | |
| B | TYR258 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:B2FSW8 |
| Chain | Residue | Details |
| A | HIS413 | |
| B | HIS413 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24478312, ECO:0007744|PDB:4OJZ |
| Chain | Residue | Details |
| A | LYS136 | |
| B | LYS198 | |
| B | LEU202 | |
| B | TYR257 | |
| B | ARG438 | |
| B | GLU667 | |
| A | GLN146 | |
| A | LYS198 | |
| A | LEU202 | |
| A | TYR257 | |
| A | ARG438 | |
| A | GLU667 | |
| B | LYS136 | |
| B | GLN146 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:24478312, ECO:0007744|PDB:4NEI, ECO:0007744|PDB:4OJZ, ECO:0007744|PDB:4OK2, ECO:0007744|PDB:4OK4 |
| Chain | Residue | Details |
| A | HIS415 | |
| A | ASP433 | |
| A | HIS464 | |
| B | HIS415 | |
| B | ASP433 | |
| B | HIS464 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | SITE: Neutralizes the sugar carboxylate group at subsite +1 => ECO:0000305|PubMed:24478312 |
| Chain | Residue | Details |
| A | ASN201 | |
| A | LEU202 | |
| B | ASN201 | |
| B | LEU202 |
