Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016740 | molecular_function | transferase activity |
| A | 0016746 | molecular_function | acyltransferase activity |
| A | 0016755 | molecular_function | aminoacyltransferase activity |
| A | 0044038 | biological_process | cell wall macromolecule biosynthetic process |
| A | 0047206 | molecular_function | UDP-N-acetylmuramoylpentapeptide-lysine N6-alanyltransferase activity |
| A | 0071555 | biological_process | cell wall organization |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | THR64 |
| A | THR66 |
| A | HOH554 |
| A | HOH607 |
| A | HOH803 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 402 |
| Chain | Residue |
| A | HOH781 |
| A | HOH850 |
| A | LEU280 |
| A | ASN283 |
| A | HOH587 |
| A | HOH665 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG A 403 |
| Chain | Residue |
| A | LEU150 |
| A | PHE308 |
| A | VAL309 |
| A | LYS310 |
| A | HOH662 |
| A | HOH829 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 404 |
| Chain | Residue |
| A | ILE54 |
| A | MET79 |
| A | ASP80 |
| A | LEU86 |
| A | ILE213 |
| A | GLU214 |
| A | HOH509 |
| A | HOH533 |
| A | HOH563 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ALA B 101 |
| Chain | Residue |
| B | UMA1 |
| B | LYS3 |
| B | HOH214 |
| site_id | AC6 |
| Number of Residues | 39 |
| Details | BINDING SITE FOR CHAIN B OF UDP-MURNAC-PENTAPEPTIDE |
| Chain | Residue |
| A | TRP32 |
| A | LYS36 |
| A | ASN38 |
| A | TRP39 |
| A | PHE70 |
| A | ASP85 |
| A | TYR103 |
| A | ARG106 |
| A | ILE142 |
| A | ILE208 |
| A | THR209 |
| A | ARG211 |
| A | PRO212 |
| A | TYR215 |
| A | TYR256 |
| A | HOH535 |
| A | HOH667 |
| B | ALA101 |
| B | HOH201 |
| B | HOH202 |
| B | HOH203 |
| B | HOH204 |
| B | HOH205 |
| B | HOH206 |
| B | HOH207 |
| B | HOH208 |
| B | HOH209 |
| B | HOH210 |
| B | HOH211 |
| B | HOH212 |
| B | HOH213 |
| B | HOH215 |
| B | HOH216 |
| B | HOH217 |
| B | HOH218 |
| B | HOH220 |
| B | HOH221 |
| B | HOH222 |
| B | HOH223 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14962386","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Site: {"description":"Important for catalytic activity","evidences":[{"source":"PubMed","id":"12679335","evidenceCode":"ECO:0000303"}]} |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 6 |
| Details | M-CSA 781 |
| Chain | Residue | Details |
| A | LYS36 | hydrogen bond donor, steric role |
| A | ASP108 | proton acceptor |
| A | ARG211 | hydrogen bond donor, steric role |
| A | PHE304 | pi-pi interaction, van der waals interaction |
| A | LYS305 | electrostatic stabiliser, hydrogen bond donor |
| A | GLU319 | hydrogen bond donor, proton acceptor, proton donor |
