2V8H
Crystal structure of mutant E159A of beta-alanine synthase from Saccharomyces kluyveri in complex with its substrate N-carbamyl-beta- alanine
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003837 | molecular_function | beta-ureidopropionase activity |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0003837 | molecular_function | beta-ureidopropionase activity |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| B | 0046872 | molecular_function | metal ion binding |
| C | 0003837 | molecular_function | beta-ureidopropionase activity |
| C | 0016787 | molecular_function | hydrolase activity |
| C | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| C | 0046872 | molecular_function | metal ion binding |
| D | 0003837 | molecular_function | beta-ureidopropionase activity |
| D | 0016787 | molecular_function | hydrolase activity |
| D | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| D | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 500 |
| Chain | Residue |
| A | HIS114 |
| A | ASP125 |
| A | GLY126 |
| A | HIS226 |
| A | URP600 |
| A | HOH3001 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS421 |
| A | URP600 |
| A | ASP125 |
| A | GLU160 |
| A | GLN229 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE URP A 600 |
| Chain | Residue |
| A | ASP125 |
| A | GLU160 |
| A | HIS226 |
| A | GLN229 |
| A | ARG322 |
| A | ALA395 |
| A | GLY396 |
| A | HIS397 |
| A | HIS421 |
| A | ZN500 |
| A | ZN501 |
| A | HOH3001 |
| B | HIS262 |
| B | ASN309 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BCN A 601 |
| Chain | Residue |
| A | VAL246 |
| A | PRO324 |
| A | VAL365 |
| A | TRP392 |
| A | HOH2301 |
| A | HOH2302 |
| A | HOH2303 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 500 |
| Chain | Residue |
| B | HIS114 |
| B | ASP125 |
| B | HIS226 |
| B | URP600 |
| B | HOH3001 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | ASP125 |
| B | GLU160 |
| B | GLN229 |
| B | HIS421 |
| B | URP600 |
| site_id | AC7 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE URP B 600 |
| Chain | Residue |
| A | HIS262 |
| A | ASN309 |
| B | ASP125 |
| B | GLU160 |
| B | GLN229 |
| B | TRP251 |
| B | ARG322 |
| B | ALA395 |
| B | GLY396 |
| B | HIS397 |
| B | HIS421 |
| B | ZN500 |
| B | ZN501 |
| site_id | AC8 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BCN B 601 |
| Chain | Residue |
| B | VAL246 |
| B | PRO324 |
| B | VAL365 |
| B | ASN366 |
| B | HOH2202 |
| B | HOH2203 |
| B | HOH2204 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN C 500 |
| Chain | Residue |
| C | HIS114 |
| C | ASP125 |
| C | HIS226 |
| C | URP600 |
| C | HOH3001 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 501 |
| Chain | Residue |
| C | ASP125 |
| C | GLU160 |
| C | HIS421 |
| C | URP600 |
| site_id | BC2 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE URP C 600 |
| Chain | Residue |
| C | ASP125 |
| C | GLU160 |
| C | HIS226 |
| C | GLN229 |
| C | TRP251 |
| C | ARG322 |
| C | ALA395 |
| C | GLY396 |
| C | HIS397 |
| C | HIS421 |
| C | ZN500 |
| C | ZN501 |
| C | HOH2048 |
| D | HIS262 |
| D | ASN309 |
| site_id | BC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BCN C 601 |
| Chain | Residue |
| C | PRO324 |
| C | ASN366 |
| C | HOH2179 |
| C | HOH2180 |
| site_id | BC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 500 |
| Chain | Residue |
| D | HIS114 |
| D | ASP125 |
| D | HIS226 |
| D | URP600 |
| D | HOH3001 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 501 |
| Chain | Residue |
| D | URP600 |
| D | ASP125 |
| D | GLU160 |
| D | GLN229 |
| D | HIS421 |
| site_id | BC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE URP D 600 |
| Chain | Residue |
| C | HIS262 |
| C | ASN309 |
| D | ASP125 |
| D | GLU160 |
| D | GLN229 |
| D | ARG322 |
| D | ALA395 |
| D | GLY396 |
| D | HIS397 |
| D | HIS421 |
| D | ZN500 |
| D | ZN501 |
| site_id | BC7 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE BCN D 601 |
| Chain | Residue |
| D | VAL246 |
| D | PRO324 |
| D | ALA364 |
| D | VAL365 |
| D | HOH2267 |
| D | HOH2268 |
| D | HOH2269 |
