1R3N
Crystal structure of beta-alanine synthase from Saccharomyces kluyveri
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 |
| E | 0003837 | molecular_function | beta-ureidopropionase activity |
| E | 0016787 | molecular_function | hydrolase activity |
| E | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| E | 0046872 | molecular_function | metal ion binding |
| F | 0003837 | molecular_function | beta-ureidopropionase activity |
| F | 0016787 | molecular_function | hydrolase activity |
| F | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| F | 0046872 | molecular_function | metal ion binding |
| G | 0003837 | molecular_function | beta-ureidopropionase activity |
| G | 0016787 | molecular_function | hydrolase activity |
| G | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| G | 0046872 | molecular_function | metal ion binding |
| H | 0003837 | molecular_function | beta-ureidopropionase activity |
| H | 0016787 | molecular_function | hydrolase activity |
| H | 0016813 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines |
| H | 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 | HIS226 |
| A | ZN501 |
| A | HOH2503 |
| A | HOH2504 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN A 501 |
| Chain | Residue |
| A | HIS421 |
| A | ZN500 |
| A | HOH2503 |
| A | ASP125 |
| A | GLU160 |
| A | GLN229 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN B 500 |
| Chain | Residue |
| B | HIS114 |
| B | ASP125 |
| B | GLU159 |
| B | HIS226 |
| B | ZN501 |
| B | HOH1503 |
| B | HOH1506 |
| site_id | AC4 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN B 501 |
| Chain | Residue |
| B | ASP125 |
| B | GLU160 |
| B | GLN229 |
| B | HIS421 |
| B | ZN500 |
| B | HOH1506 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 500 |
| Chain | Residue |
| C | HIS114 |
| C | ASP125 |
| C | HIS226 |
| C | ZN501 |
| C | HOH3503 |
| C | HOH3504 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN C 501 |
| Chain | Residue |
| C | ASP125 |
| C | GLU160 |
| C | GLN229 |
| C | HIS421 |
| C | ZN500 |
| C | HOH3503 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN D 500 |
| Chain | Residue |
| D | HIS114 |
| D | ASP125 |
| D | HIS226 |
| D | ZN501 |
| D | HOH4503 |
| D | HOH4504 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN D 501 |
| Chain | Residue |
| D | ASP125 |
| D | GLU160 |
| D | HIS421 |
| D | ZN500 |
| D | HOH4503 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN E 500 |
| Chain | Residue |
| E | HIS114 |
| E | ASP125 |
| E | GLU159 |
| E | HIS226 |
| E | ZN501 |
| E | HOH6503 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN E 501 |
| Chain | Residue |
| E | ASP125 |
| E | GLU160 |
| E | HIS421 |
| E | ZN500 |
| E | HOH6503 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN F 500 |
| Chain | Residue |
| F | HIS114 |
| F | ASP125 |
| F | HIS226 |
| F | ZN501 |
| F | HOH502 |
| F | HOH504 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN F 501 |
| Chain | Residue |
| F | ASP125 |
| F | GLU160 |
| F | GLN229 |
| F | HIS421 |
| F | ZN500 |
| F | HOH504 |
| site_id | BC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE ZN G 500 |
| Chain | Residue |
| G | HIS114 |
| G | ASP125 |
| G | GLY126 |
| G | HIS226 |
| G | ZN501 |
| G | HOH8503 |
| G | HOH8504 |
| site_id | BC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN G 501 |
| Chain | Residue |
| G | ASP125 |
| G | GLU160 |
| G | HIS421 |
| G | ZN500 |
| G | HOH8503 |
| site_id | BC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN H 500 |
| Chain | Residue |
| H | HIS114 |
| H | ASP125 |
| H | HIS226 |
| H | ZN501 |
| H | HOH502 |
| H | HOH503 |
| site_id | BC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE ZN H 501 |
| Chain | Residue |
| H | ASP125 |
| H | GLU160 |
| H | GLN229 |
| H | HIS421 |
| H | ZN500 |
| H | HOH502 |
| site_id | BC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BIB B 1502 |
| Chain | Residue |
| B | HIS262 |
| B | ASN309 |
| A | TRP251 |
| A | ARG322 |
| A | GLY396 |
| A | HOH2508 |
| site_id | BC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BIB A 2502 |
| Chain | Residue |
| A | HIS262 |
| A | ASN309 |
| B | TYR249 |
| B | ARG322 |
| B | GLY396 |
| site_id | CC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BIB C 3502 |
| Chain | Residue |
| C | TRP251 |
| C | ARG322 |
| C | GLY396 |
| D | HIS262 |
| D | ASN309 |
| site_id | CC2 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE BIB D 4502 |
| Chain | Residue |
| C | HIS262 |
| C | ASN309 |
| D | SER167 |
| D | TYR249 |
| D | TRP251 |
| D | ARG322 |
| D | ALA395 |
| D | GLY396 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BIB E 5502 |
| Chain | Residue |
| E | TYR249 |
| E | TRP251 |
| E | ARG322 |
| E | ALA395 |
| E | GLY396 |
| F | ASN309 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE BIB E 6502 |
| Chain | Residue |
| E | HIS262 |
| E | ASN309 |
| F | TYR249 |
| F | ARG322 |
| F | GLY396 |
| site_id | CC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BIB G 7502 |
| Chain | Residue |
| G | ARG322 |
| G | GLY396 |
| H | HIS262 |
| H | ASN309 |
| site_id | CC6 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE BIB G 8502 |
| Chain | Residue |
| G | HIS262 |
| G | ASN309 |
| H | ARG322 |
| H | GLY396 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| A | GLU159 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| B | GLU159 |
| site_id | CSA3 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| C | GLU159 |
| site_id | CSA4 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| D | GLU159 |
| site_id | CSA5 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| E | GLU159 |
| site_id | CSA6 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| F | GLU159 |
| site_id | CSA7 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| G | GLU159 |
| site_id | CSA8 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1amp |
| Chain | Residue | Details |
| H | GLU159 |
