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5U2G

2.6 Angstrom Resolution Crystal Structure of Penicillin-Binding Protein 1A from Haemophilus influenzae

Functional Information from GO Data
ChainGOidnamespacecontents
A0004180molecular_functioncarboxypeptidase activity
A0005886cellular_componentplasma membrane
A0006508biological_processproteolysis
A0008360biological_processregulation of cell shape
A0008658molecular_functionpenicillin binding
A0008955molecular_functionpeptidoglycan glycosyltransferase activity
A0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
A0009252biological_processpeptidoglycan biosynthetic process
A0016757molecular_functionglycosyltransferase activity
A0046677biological_processresponse to antibiotic
A0071555biological_processcell wall organization
B0004180molecular_functioncarboxypeptidase activity
B0005886cellular_componentplasma membrane
B0006508biological_processproteolysis
B0008360biological_processregulation of cell shape
B0008658molecular_functionpenicillin binding
B0008955molecular_functionpeptidoglycan glycosyltransferase activity
B0009002molecular_functionserine-type D-Ala-D-Ala carboxypeptidase activity
B0009252biological_processpeptidoglycan biosynthetic process
B0016757molecular_functionglycosyltransferase activity
B0046677biological_processresponse to antibiotic
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 A 901
ChainResidue
ALYS204
AARG221
AARG228

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 902
ChainResidue
AARG384
ASER385
AASN386

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 903
ChainResidue
AHOH1055
AILE478
ASER479
AARG517

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 904
ChainResidue
ATRP714
AARG715

site_idAC5
Number of Residues5
Detailsbinding site for residue SO4 A 905
ChainResidue
AASP296
AGLU427
AASP786
ALYS787
AHOH1053

site_idAC6
Number of Residues3
Detailsbinding site for residue SO4 A 906
ChainResidue
AARG561
AHOH1056
AHOH1116

site_idAC7
Number of Residues1
Detailsbinding site for residue SO4 A 907
ChainResidue
AARG274

site_idAC8
Number of Residues1
Detailsbinding site for residue SO4 A 908
ChainResidue
AARG335

site_idAC9
Number of Residues1
Detailsbinding site for residue CL A 910
ChainResidue
ATHR731

site_idAD1
Number of Residues3
Detailsbinding site for residue CL A 911
ChainResidue
AARG275
AILE577
AILE578

site_idAD2
Number of Residues2
Detailsbinding site for residue CL A 912
ChainResidue
AGLN297
AGLN301

site_idAD3
Number of Residues3
Detailsbinding site for residue PEG A 914
ChainResidue
ASER785
ALYS787
APRO788

site_idAD4
Number of Residues3
Detailsbinding site for residue SO4 B 901
ChainResidue
BLYS204
BARG221
BARG228

site_idAD5
Number of Residues3
Detailsbinding site for residue SO4 B 902
ChainResidue
BARG384
BSER385
BASN386

site_idAD6
Number of Residues4
Detailsbinding site for residue SO4 B 903
ChainResidue
BASP296
BGLU427
BASP786
BLYS787

site_idAD7
Number of Residues3
Detailsbinding site for residue SO4 B 904
ChainResidue
BILE478
BSER479
BARG517

site_idAD8
Number of Residues3
Detailsbinding site for residue SO4 B 905
ChainResidue
BTRP714
BARG715
BHOH1109

site_idAD9
Number of Residues3
Detailsbinding site for residue SO4 B 906
ChainResidue
BTYR702
BARG722
BHOH1003

site_idAE1
Number of Residues1
Detailsbinding site for residue SO4 B 907
ChainResidue
BARG335

site_idAE2
Number of Residues4
Detailsbinding site for residue SO4 B 908
ChainResidue
BARG561
BLEU572
BHOH1043
BHOH1122

site_idAE3
Number of Residues1
Detailsbinding site for residue CL B 910
ChainResidue
BTHR731

site_idAE4
Number of Residues3
Detailsbinding site for residue CL B 911
ChainResidue
BARG275
BILE577
BILE578

site_idAE5
Number of Residues3
Detailsbinding site for residue CL B 912
ChainResidue
BTYR263
BGLN297
BGLN301

site_idAE6
Number of Residues2
Detailsbinding site for residue CL B 913
ChainResidue
BLYS587
BLEU589

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor; for transglycosylase activity => ECO:0000250|UniProtKB:P02919
ChainResidueDetails
AGLU86
BGLU86

site_idSWS_FT_FI2
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate; for transpeptidase activity => ECO:0000250|UniProtKB:P02919
ChainResidueDetails
ASER452
BSER452

225946

PDB entries from 2024-10-09

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