1E4E
D-alanyl-D-lacate ligase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0008360 | biological_process | regulation of cell shape |
| A | 0008716 | molecular_function | D-alanine-D-alanine ligase activity |
| A | 0009252 | biological_process | peptidoglycan biosynthetic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046677 | biological_process | response to antibiotic |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071555 | biological_process | cell wall organization |
| A | 0160220 | molecular_function | D-alanine-(R)-lactate ligase activity |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0008360 | biological_process | regulation of cell shape |
| B | 0008716 | molecular_function | D-alanine-D-alanine ligase activity |
| B | 0009252 | biological_process | peptidoglycan biosynthetic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0046677 | biological_process | response to antibiotic |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071555 | biological_process | cell wall organization |
| B | 0160220 | molecular_function | D-alanine-(R)-lactate ligase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE ADP A 350 |
| Chain | Residue |
| A | LYS133 |
| A | VAL210 |
| A | GLU214 |
| A | LEU236 |
| A | ILE240 |
| A | PHE241 |
| A | PHE294 |
| A | ASN304 |
| A | GLU305 |
| A | PHY355 |
| A | MG360 |
| A | PHE169 |
| A | MG365 |
| A | HOH2095 |
| A | HOH2112 |
| A | HOH2151 |
| A | HOH2166 |
| A | HOH2167 |
| A | LYS171 |
| A | SER175 |
| A | GLY176 |
| A | SER177 |
| A | SER178 |
| A | GLU207 |
| A | GLN208 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE PHY A 355 |
| Chain | Residue |
| A | GLU16 |
| A | SER177 |
| A | PHE241 |
| A | ILE243 |
| A | HIS244 |
| A | ARG290 |
| A | GLU305 |
| A | ASN307 |
| A | GLY311 |
| A | SER316 |
| A | ARG317 |
| A | ADP350 |
| A | MG360 |
| A | MG365 |
| A | HOH2097 |
| A | HOH2154 |
| A | HOH2167 |
| A | HOH2168 |
| A | HOH2169 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 360 |
| Chain | Residue |
| A | GLU305 |
| A | ASN307 |
| A | ADP350 |
| A | PHY355 |
| A | HOH2095 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 365 |
| Chain | Residue |
| A | GLU305 |
| A | ADP350 |
| A | PHY355 |
| A | HOH2151 |
| A | HOH2167 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ADP B 350 |
| Chain | Residue |
| B | LYS133 |
| B | PHE169 |
| B | LYS171 |
| B | GLY176 |
| B | SER177 |
| B | SER178 |
| B | GLU207 |
| B | GLN208 |
| B | ALA209 |
| B | VAL210 |
| B | GLU214 |
| B | LEU236 |
| B | ILE240 |
| B | PHE241 |
| B | PHE294 |
| B | ASN304 |
| B | GLU305 |
| B | PHY355 |
| B | MG360 |
| B | MG365 |
| B | HOH2150 |
| B | HOH2171 |
| B | HOH2172 |
| site_id | AC6 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE PHY B 355 |
| Chain | Residue |
| B | GLU16 |
| B | SER177 |
| B | HIS244 |
| B | ARG290 |
| B | GLU305 |
| B | ASN307 |
| B | GLY311 |
| B | SER316 |
| B | ARG317 |
| B | ADP350 |
| B | MG360 |
| B | MG365 |
| B | HOH2054 |
| B | HOH2096 |
| B | HOH2160 |
| B | HOH2171 |
| B | HOH2173 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE MG B 360 |
| Chain | Residue |
| B | HOH2094 |
| B | GLY176 |
| B | GLU305 |
| B | ASN307 |
| B | ADP350 |
| B | PHY355 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG B 365 |
| Chain | Residue |
| B | GLU305 |
| B | ADP350 |
| B | PHY355 |
| B | HOH2150 |
| B | HOH2171 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1342 |
| Chain | Residue |
| A | HOH2143 |
| B | ARG174 |
| B | LYS203 |
| B | HOH2103 |
| B | HOH3002 |
| site_id | BC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1343 |
| Chain | Residue |
| A | ARG174 |
| A | LYS203 |
| A | HOH2109 |
| A | HOH3003 |
| A | HOH3004 |
| B | HOH2068 |
| site_id | BC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1344 |
| Chain | Residue |
| A | ASP105 |
| A | ARG174 |
| A | HOH3007 |
| A | HOH3008 |
| B | GLN125 |
| B | HOH3009 |
| B | HOH3010 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 1345 |
| Chain | Residue |
| A | SER66 |
| A | LYS81 |
| A | ARG242 |
| A | GLN245 |
| A | GLU246 |
| A | VAL247 |
| site_id | BC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL B 1343 |
| Chain | Residue |
| B | SER265 |
| B | ALA266 |
| site_id | BC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1344 |
| Chain | Residue |
| B | ARG3 |
| B | LYS33 |
| B | GLU34 |
| site_id | BC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 1345 |
| Chain | Residue |
| B | LEU339 |
| B | ALA340 |
| B | LEU341 |
| site_id | BC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1346 |
| Chain | Residue |
| A | GLU62 |
| A | LYS183 |
| A | TYR238 |
| A | GLY239 |
| site_id | BC8 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 1347 |
| Chain | Residue |
| A | HIS84 |
| A | SER178 |
| A | ARG242 |
| A | GLN245 |
| site_id | BC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GOL A 1348 |
| Chain | Residue |
| A | ASN2 |
| A | ARG3 |
| site_id | CC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1349 |
| Chain | Residue |
| A | LYS155 |
| A | GLU195 |
| A | HOH2106 |
| site_id | CC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1346 |
| Chain | Residue |
| B | GLU37 |
| B | LEU39 |
| B | MET51 |
| B | ASN89 |
| site_id | CC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL B 1347 |
| Chain | Residue |
| B | GLU26 |
| B | PHE312 |
| B | THR313 |
| B | SER314 |
| B | LEU329 |
| B | HOH3011 |
| site_id | CC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 990 |
| Chain | Residue |
| A | GLU62 |
| A | ASN63 |
| A | CYS64 |
| A | TYR65 |
| A | SER66 |
| site_id | CC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 996 |
| Chain | Residue |
| A | LYS155 |
| site_id | CC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 1350 |
| Chain | Residue |
| A | LYS5 |
| A | GLU37 |
| A | ASN89 |
| site_id | CC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL B 1348 |
| Chain | Residue |
| B | LYS50 |
| B | TYR65 |
| B | HOH3012 |
| B | HOH3013 |
Functional Information from PROSITE/UniProt
| site_id | PS00843 |
| Number of Residues | 12 |
| Details | DALA_DALA_LIGASE_1 D-alanine--D-alanine ligase signature 1. HGksGEDGsIQG |
| Chain | Residue | Details |
| B | HIS99-GLY110 | |
| A | HIS99-GLY110 |
| site_id | PS00844 |
| Number of Residues | 29 |
| Details | DALA_DALA_LIGASE_2 D-alanine--D-alanine ligase signature 2. LgcrGlARVDMFlqdrgriv....LnEVNTlPG |
| Chain | Residue | Details |
| B | LEU283-GLY311 | |
| A | LEU283-GLY311 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 402 |
| Details | Domain: {"description":"ATP-grasp"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 28 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"10908650","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 8 |
| Details | M-CSA 310 |
| Chain | Residue | Details |
| B | VAL19 | electrostatic stabiliser, steric role |
| B | LYS22 | hydrogen bond donor, increase basicity |
| B | HIS99 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| B | HIS244 | attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor |
| B | GLU250 | hydrogen bond acceptor, increase basicity |
| B | ARG290 | attractive charge-charge interaction, electrostatic stabiliser |
| B | GLY311 | electrostatic stabiliser, hydrogen bond donor |
| B | TYR315 | hydrogen bond donor, increase basicity |
