Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3R5X

Crystal Structure of D-alanine--D-Alanine Ligase from Bacillus anthracis complexed with ATP

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
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
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
C0003824molecular_functioncatalytic activity
C0005524molecular_functionATP binding
C0005737cellular_componentcytoplasm
C0008360biological_processregulation of cell shape
C0008716molecular_functionD-alanine-D-alanine ligase activity
C0009252biological_processpeptidoglycan biosynthetic process
C0016874molecular_functionligase activity
C0046872molecular_functionmetal ion binding
C0071555biological_processcell wall organization
D0003824molecular_functioncatalytic activity
D0005524molecular_functionATP binding
D0005737cellular_componentcytoplasm
D0008360biological_processregulation of cell shape
D0008716molecular_functionD-alanine-D-alanine ligase activity
D0009252biological_processpeptidoglycan biosynthetic process
D0016874molecular_functionligase activity
D0046872molecular_functionmetal ion binding
D0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CA A 401
ChainResidue
AASP248
AGLU260
AATP402
AHOH706

site_idAC2
Number of Residues18
DetailsBINDING SITE FOR RESIDUE ATP A 402
ChainResidue
ALYS173
ATYR174
AILE175
AGLU179
AMSE259
AGLU260
AASN262
ACA401
AHOH573
AHOH598
AHOH687
AHOH688
AHOH706
ALYS95
AVAL134
ALYS136
AVAL146
AGLU172

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CA B 401
ChainResidue
BASP248
BGLU260
BATP402

site_idAC4
Number of Residues17
DetailsBINDING SITE FOR RESIDUE ATP B 402
ChainResidue
BGLU66
BLYS95
BVAL134
BLYS136
BGLY145
BVAL146
BGLU172
BLYS173
BTYR174
BILE175
BGLU179
BMSE250
BMSE259
BGLU260
BASN262
BCA401
BHOH651

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE CA B 403
ChainResidue
AASN31
AHOH681
BGLY281
BHOH619
BHOH620
BHOH621
BHOH622

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 401
ChainResidue
CARG246
CASP248
CGLU260
CATP402
CHOH616

site_idAC7
Number of Residues16
DetailsBINDING SITE FOR RESIDUE ATP C 402
ChainResidue
CLYS63
CLYS95
CVAL134
CLYS136
CVAL146
CGLU172
CLYS173
CTYR174
CILE175
CGLU179
CMSE250
CMSE259
CGLU260
CCA401
CHOH616
CHOH618

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CA C 403
ChainResidue
APHE131
AHOH629
AHOH686
CGLU108
CHOH637

site_idAC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE MG C 404
ChainResidue
CARG299
CGLU302
CHOH643
CHOH644
CHOH645

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 401
ChainResidue
AASP203
AHOH525
DASP248
DGLU260
DATP402
DHOH660

site_idBC2
Number of Residues26
DetailsBINDING SITE FOR RESIDUE ATP D 402
ChainResidue
DGLU179
DMSE250
DMSE259
DGLU260
DASN262
DCA401
DHOH527
DHOH615
DHOH625
DHOH660
DHOH677
DHOH691
DHOH700
APHE201
AASP203
AHOH525
AHOH569
AHOH661
DLYS95
DVAL134
DLYS136
DVAL146
DGLU172
DLYS173
DTYR174
DILE175

site_idBC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CA D 403
ChainResidue
AASP253
DGLU200
DASP203
DTYR208
DHOH667
DHOH668

site_idBC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO D 404
ChainResidue
DGLU75
DARG299
DGLU302
DPHE304
DHOH726

site_idBC5
Number of Residues2
DetailsBINDING SITE FOR RESIDUE ACY D 405
ChainResidue
DASP111
DHOH623

Functional Information from PROSITE/UniProt
site_idPS00843
Number of Residues12
DetailsDALA_DALA_LIGASE_1 D-alanine--D-alanine ligase signature 1. HGkyGEDGtVQG
ChainResidueDetails
AHIS61-GLY72

site_idPS00844
Number of Residues28
DetailsDALA_DALA_LIGASE_2 D-alanine--D-alanine ligase signature 2. LkcsVyARVDMMvkdgipy.....VmEVNTlPG
ChainResidueDetails
ALEU239-GLY266

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues16
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00047
ChainResidueDetails
ALEU126
CASP248
CGLU260
CASN262
DLEU126
DASP248
DGLU260
DASN262
AASP248
AGLU260
AASN262
BLEU126
BASP248
BGLU260
BASN262
CLEU126

227111

PDB entries from 2024-11-06

PDB statisticsPDBj update infoContact PDBjnumon