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2AWD

Crystal structure of LacC from Enterococcus faecalis

Functional Information from GO Data
ChainGOidnamespacecontents
A0005524molecular_functionATP binding
A0005829cellular_componentcytosol
A0005975biological_processcarbohydrate metabolic process
A0005988biological_processlactose metabolic process
A0008443molecular_functionphosphofructokinase activity
A0009024molecular_functiontagatose-6-phosphate kinase activity
A0016301molecular_functionkinase activity
A0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
A0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
A0046835biological_processcarbohydrate phosphorylation
A2001059biological_processD-tagatose 6-phosphate catabolic process
B0005524molecular_functionATP binding
B0005829cellular_componentcytosol
B0005975biological_processcarbohydrate metabolic process
B0005988biological_processlactose metabolic process
B0008443molecular_functionphosphofructokinase activity
B0009024molecular_functiontagatose-6-phosphate kinase activity
B0016301molecular_functionkinase activity
B0016772molecular_functiontransferase activity, transferring phosphorus-containing groups
B0016773molecular_functionphosphotransferase activity, alcohol group as acceptor
B0046835biological_processcarbohydrate phosphorylation
B2001059biological_processD-tagatose 6-phosphate catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 401
ChainResidue
ALYS38
AARG88
ASER136

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR B 402
ChainResidue
BLYS38
BARG88
BSER136

site_idAC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR A 403
ChainResidue
AALA312

site_idAC4
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR A 404
ChainResidue
AARG44

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR B 405
ChainResidue
BSER168
BLEU169
BTHR164

site_idAC6
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR B 406
ChainResidue
BPRO212
BMSE213

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR B 407
ChainResidue
BALA105
BGLY106

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 408
ChainResidue
AALA105
AGLY106

site_idAC9
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR B 409
ChainResidue
BARG44

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BR A 410
ChainResidue
AGLN174
AHOH584

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE BR A 411
ChainResidue
AALA312
ALYS313
BGLN307

site_idBC3
Number of Residues1
DetailsBINDING SITE FOR RESIDUE BR A 412
ChainResidue
AHOH562

Functional Information from PROSITE/UniProt
site_idPS00583
Number of Residues25
DetailsPFKB_KINASES_1 pfkB family of carbohydrate kinases signature 1. GGkGlNVTrvIhDLGgdviatgvlG
ChainResidueDetails
AGLY36-GLY60

site_idPS00584
Number of Residues14
DetailsPFKB_KINASES_2 pfkB family of carbohydrate kinases signature 2. NPvGSGDatiAGLA
ChainResidueDetails
AASN249-ALA262

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
AGLY254
AASP255
ASER253
AGLY252

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1tz3
ChainResidueDetails
BGLY254
BASP255
BSER253
BGLY252

227344

PDB entries from 2024-11-13

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