1WTC
Crystal Structure of S.pombe Serine Racemase complex with AMPPCP
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 | 0006563 | biological_process | L-serine 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 |
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 | HOH468 |
| A | HOH489 |
| A | HOH494 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 380 |
| Chain | Residue |
| A | HOH528 |
| A | HOH547 |
| A | ACP370 |
| A | HOH431 |
| A | HOH454 |
| site_id | AC3 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE PLP A 350 |
| Chain | Residue |
| A | PHE56 |
| A | LYS57 |
| A | ASN84 |
| A | GLY183 |
| A | GLY184 |
| A | GLY185 |
| A | GLY186 |
| A | LEU187 |
| A | GLY236 |
| A | GLU281 |
| A | THR283 |
| A | SER308 |
| A | HOH403 |
| A | HOH419 |
| A | HOH430 |
| A | HOH614 |
| site_id | AC4 |
| Number of Residues | 29 |
| Details | BINDING SITE FOR RESIDUE ACP A 370 |
| Chain | Residue |
| A | ASN25 |
| A | THR31 |
| A | SER32 |
| A | SER33 |
| A | THR34 |
| A | LYS52 |
| A | MET53 |
| A | ALA111 |
| A | ALA114 |
| A | ALA115 |
| A | TYR119 |
| A | ALA274 |
| A | ARG275 |
| A | LYS277 |
| A | ASN311 |
| A | MG380 |
| A | HOH382 |
| A | HOH394 |
| A | HOH414 |
| A | HOH417 |
| A | HOH426 |
| A | HOH431 |
| A | HOH438 |
| A | HOH528 |
| A | HOH581 |
| A | HOH588 |
| A | HOH615 |
| A | HOH616 |
| A | HOH618 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000269|PubMed:19640845, ECO:0007744|PDB:2ZR8 |
| Chain | Residue | Details |
| A | LYS57 | |
| A | SER82 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:Q9GZT4 |
| Chain | Residue | Details |
| A | SER32 | |
| A | ASP214 | |
| A | LYS277 | |
| A | ASN311 | |
| A | SER33 | |
| A | LYS52 | |
| A | THR79 | |
| A | GLN87 | |
| A | TYR119 | |
| A | ASP176 | |
| A | GLU208 | |
| A | GLY212 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 7 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC |
| Chain | Residue | Details |
| A | ASN84 | |
| A | GLY183 | |
| A | GLY184 | |
| A | GLY185 | |
| A | GLY186 | |
| A | LEU187 | |
| A | SER308 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-(pyridoxal phosphate)lysine; alternate => ECO:0000269|PubMed:19155267, ECO:0000269|PubMed:19640845, ECO:0000269|Ref.2, ECO:0007744|PDB:1V71, ECO:0007744|PDB:1WTC |
| Chain | Residue | Details |
| A | LYS57 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | LYS57 | |
| A | THR283 |
| site_id | CSA2 |
| Number of Residues | 1 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | LYS57 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1oas |
| Chain | Residue | Details |
| A | LYS57 | |
| A | SER308 |
| 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 |
