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

4BUB

CRYSTAL STRUCTURE OF MURE LIGASE FROM THERMOTOGA MARITIMA IN COMPLEX WITH ADP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0004326molecular_functiontetrahydrofolylpolyglutamate synthase activity
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0007049biological_processcell cycle
A0008360biological_processregulation of cell shape
A0009058biological_processbiosynthetic process
A0009252biological_processpeptidoglycan biosynthetic process
A0009396biological_processfolic acid-containing compound biosynthetic process
A0016874molecular_functionligase activity
A0016881molecular_functionacid-amino acid ligase activity
A0046901biological_processtetrahydrofolylpolyglutamate biosynthetic process
A0047482molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity
A0051301biological_processcell division
A0071555biological_processcell wall organization
A0102195molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--D-lysine ligase activity
B0000166molecular_functionnucleotide binding
B0000287molecular_functionmagnesium ion binding
B0004326molecular_functiontetrahydrofolylpolyglutamate synthase activity
B0005524molecular_functionATP binding
B0005737cellular_componentcytoplasm
B0007049biological_processcell cycle
B0008360biological_processregulation of cell shape
B0009058biological_processbiosynthetic process
B0009252biological_processpeptidoglycan biosynthetic process
B0009396biological_processfolic acid-containing compound biosynthetic process
B0016874molecular_functionligase activity
B0016881molecular_functionacid-amino acid ligase activity
B0046901biological_processtetrahydrofolylpolyglutamate biosynthetic process
B0047482molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamate-L-lysine ligase activity
B0051301biological_processcell division
B0071555biological_processcell wall organization
B0102195molecular_functionUDP-N-acetylmuramoyl-L-alanyl-D-glutamate--D-lysine ligase activity
Functional Information from PDB Data
site_idAC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE ADP A 1486
ChainResidue
ATHR111
AALA351
ALYS354
AMG1487
AASN112
AGLY113
ALYS114
ATHR115
ATHR116
AASN200
AASN296
AARG327

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 1487
ChainResidue
ATHR137
AGLU177
AADP1486

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE ADP B 1486
ChainResidue
BTHR111
BASN112
BGLY113
BLYS114
BTHR115
BGLU177
BASN200
BPHE292
BASN296
BARG327
BMG1487

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 1487
ChainResidue
BTHR115
BTHR137
BADP1486

Functional Information from PROSITE/UniProt
site_idPS01011
Number of Residues24
DetailsFOLYLPOLYGLU_SYNT_1 Folylpolyglutamate synthase signature 1. FgVTGTNGKtTttmmIyHMLtsl.G
ChainResidueDetails
APHE106-GLY129

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues10
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
ASER32
BARG187
ATHR152
ASER179
AGLN185
AARG187
BSER32
BTHR152
BSER179
BGLN185

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255
ChainResidueDetails
AGLY110
BGLY110

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000250
ChainResidueDetails
ALYS219
BLYS219

218853

PDB entries from 2024-04-24

PDB statisticsPDBj update infoContact PDBjnumon