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4FU0

Crystal Structure of VanG D-Ala:D-Ser Ligase from Enterococcus faecalis

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0008360biological_processregulation of cell shape
A0008716molecular_functionD-alanine-D-alanine ligase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016874molecular_functionligase activity
A0046872molecular_functionmetal ion binding
A0071555biological_processcell wall organization
B0003824molecular_functioncatalytic activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0008360biological_processregulation of cell shape
B0008716molecular_functionD-alanine-D-alanine ligase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016874molecular_functionligase activity
B0046872molecular_functionmetal ion binding
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues21
DetailsBINDING SITE FOR RESIDUE ADP A 401
ChainResidue
ALYS140
AGLU226
ALEU247
ATYR258
ALYS261
APHE301
AASN311
AGLU312
AHOH556
AHOH588
AHOH593
APHE181
AHOH637
BTYR258
ALYS183
ASER190
AILE193
AGLU219
AGLU220
ATHR221
AILE222

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 402
ChainResidue
AARG297
AASN314
APRO317
AGLY318
AHOH501
AHOH525
AHOH575
BLYS257

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 403
ChainResidue
AASN223
ATHR303
APRO304
ASER305

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 404
ChainResidue
ASER335
APHE336
AHOH611
AHOH612

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 405
ChainResidue
ALYS108
AGLY188
ASER189
AHOH640

site_idAC6
Number of Residues19
DetailsBINDING SITE FOR RESIDUE ADP B 401
ChainResidue
BPHE181
BLYS183
BSER190
BILE193
BGLU219
BGLU220
BTHR221
BILE222
BGLU226
BLEU247
BPHE252
BPHE301
BASN311
BGLU312
BHOH503
BHOH529
BHOH540
BHOH617
BHOH649

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 402
ChainResidue
BARG297
BGLY318
BSER323
BARG324
BHOH501
BHOH514
BHOH633
BHOH641

site_idAC8
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 403
ChainResidue
BASN223
BTHR303
BPRO304
BSER305
BHOH594
BHOH600

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 404
ChainResidue
ATYR254
BALA187
BGLY188
BSER189
BHIS212

site_idBC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 405
ChainResidue
ALYS330
BLYS264
BTYR266
BARG270

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 406
ChainResidue
BLYS330
BSER335
BPHE336

Functional Information from PROSITE/UniProt
site_idPS00843
Number of Residues12
DetailsDALA_DALA_LIGASE_1 D-alanine--D-alanine ligase signature 1. HGknGEDGtLQG
ChainResidueDetails
AHIS106-GLY117

site_idPS00844
Number of Residues29
DetailsDALA_DALA_LIGASE_2 D-alanine--D-alanine ligase signature 2. LgcsGfSRVDMFytpsgeiv....FnEVNTiPG
ChainResidueDetails
ALEU290-GLY318

219140

PDB entries from 2024-05-01

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