2ZPU
Crystal Structure of Modified Serine Racemase from S.pombe.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0003941 | molecular_function | L-serine ammonia-lyase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005575 | cellular_component | cellular_component |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0006563 | biological_process | L-serine metabolic process |
| A | 0008152 | biological_process | metabolic process |
| A | 0008721 | molecular_function | D-serine ammonia-lyase activity |
| A | 0016829 | molecular_function | lyase activity |
| A | 0016853 | molecular_function | isomerase activity |
| A | 0018114 | molecular_function | threonine racemase activity |
| A | 0030170 | molecular_function | pyridoxal phosphate binding |
| A | 0030378 | molecular_function | serine racemase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0070178 | biological_process | D-serine metabolic process |
| A | 0070179 | biological_process | D-serine biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 360 |
| Chain | Residue |
| A | GLU208 |
| A | GLY212 |
| A | ASP214 |
| A | HOH362 |
| A | HOH363 |
| A | HOH376 |
| site_id | AC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE PDD A 350 |
| Chain | Residue |
| A | SER82 |
| A | ASN84 |
| A | HIS85 |
| A | PRO151 |
| A | CYS181 |
| A | GLY183 |
| A | GLY184 |
| A | GLY185 |
| A | GLY186 |
| A | LEU187 |
| A | GLY236 |
| A | GLU281 |
| A | THR283 |
| A | SER308 |
| A | HOH369 |
| A | HOH370 |
| A | HOH371 |
| A | HOH374 |
| A | HOH384 |
| A | PHE56 |
| A | LYS57 |
| A | SER81 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | LYS57 | |
| A | SER82 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | ASN25 | |
| A | LYS52 | |
| A | MET53 | |
| A | TYR119 | |
| A | ARG133 | |
| A | GLU208 | |
| A | GLY212 | |
| A | ASP214 | |
| A | ASP235 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine; alternate |
| Chain | Residue | Details |
| A | LYS57 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 330 |
| Chain | Residue | Details |
| A | LYS57 | activator, covalently attached, electron pair acceptor, electron pair donor, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | SER82 | electrostatic stabiliser, hydrogen bond acceptor, proton acceptor, proton donor |
| A | GLU208 | metal ligand |
| A | GLY212 | metal ligand |
| A | ASP214 | metal ligand |
| A | SER308 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond acceptor |
| site_id | MCSA2 |
| Number of Residues | 6 |
| Details | M-CSA 956 |
| Chain | Residue | Details |
| A | LYS57 | covalently attached, electron pair acceptor, electron pair donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | SER82 | electrostatic stabiliser |
| A | GLU208 | metal ligand |
| A | GLY212 | metal ligand |
| A | ASP214 | metal ligand |
| A | SER308 | electrostatic stabiliser |
