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6NKJ

1.3 Angstrom Resolution Crystal Structure of UDP-N-acetylglucosamine 1-carboxyvinyltransferase from Streptococcus pneumoniae in Complex with (2R)-2-(phosphonooxy)propanoic acid.

Functional Information from GO Data
ChainGOidnamespacecontents
A0003824molecular_functioncatalytic activity
A0005737cellular_componentcytoplasm
A0007049biological_processcell cycle
A0008360biological_processregulation of cell shape
A0008760molecular_functionUDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016740molecular_functiontransferase activity
A0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
A0019277biological_processUDP-N-acetylgalactosamine biosynthetic process
A0051301biological_processcell division
A0071555biological_processcell wall organization
B0003824molecular_functioncatalytic activity
B0005737cellular_componentcytoplasm
B0007049biological_processcell cycle
B0008360biological_processregulation of cell shape
B0008760molecular_functionUDP-N-acetylglucosamine 1-carboxyvinyltransferase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016740molecular_functiontransferase activity
B0016765molecular_functiontransferase activity, transferring alkyl or aryl (other than methyl) groups
B0019277biological_processUDP-N-acetylgalactosamine biosynthetic process
B0051301biological_processcell division
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues9
Detailsbinding site for residue 0V5 A 501
ChainResidue
AARG96
ACYS120
ATHR121
AARG401
ACIT502
AHOH609
AHOH642
AHOH679
AHOH790

site_idAC2
Number of Residues19
Detailsbinding site for residue CIT A 502
ChainResidue
ALYS23
AASN24
AILE122
AARG125
AASP309
AARG335
ALEU374
AARG375
AARG401
A0V5501
AHOH636
AHOH647
AHOH652
AHOH670
AHOH736
AHOH742
AHOH865
AHOH1066
AHOH1154

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 503
ChainResidue
ASER115
AGLY146
ATYR147
BARG344

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO B 502
ChainResidue
BHIS226
BLYS299
BHOH908
BHOH952
BHOH1058

site_idAC5
Number of Residues25
Detailsbinding site for residue CIT B 503
ChainResidue
BLYS23
BASN24
BILE122
BARG125
BASP309
BPHE332
BARG335
BLEU374
BARG375
BARG401
B0V5501
BHOH633
BHOH638
BHOH665
BHOH705
BHOH716
BHOH746
BHOH774
BHOH779
BHOH827
BHOH912
BHOH927
BHOH1039
BHOH1091
BHOH1169

site_idAC6
Number of Residues1
Detailsbinding site for residue CL B 504
ChainResidue
BASN203

site_idAC7
Number of Residues14
Detailsbinding site for Di-peptide 0V5 B 501 and CYS B 120
ChainResidue
AGLU340
AHOH646
BARG96
BGLY119
BTHR121
BILE122
BGLY123
BARG125
BARG401
BCIT503
BHOH674
BHOH679
BHOH686
BHOH776

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
ACYS120
BCYS120

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
ALYS23
BVAL331
AARG96
AARG125
AASP309
AVAL331
BLYS23
BARG96
BARG125
BASP309

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: 2-(S-cysteinyl)pyruvic acid O-phosphothioketal => ECO:0000255|HAMAP-Rule:MF_00111
ChainResidueDetails
ACYS120
BCYS120

218853

건을2024-04-24부터공개중

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