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5KSH

Crystal structure of penicillin-binding protein 2 from Neisseria gonorrhoeae containing an A501T mutation associated with cephalosporin resistance

Functional Information from GO Data
ChainGOidnamespacecontents
A0000917biological_processdivision septum assembly
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
A0043093biological_processFtsZ-dependent cytokinesis
A0046677biological_processresponse to antibiotic
A0051301biological_processcell division
A0071555biological_processcell wall organization
B0000917biological_processdivision septum assembly
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
B0043093biological_processFtsZ-dependent cytokinesis
B0046677biological_processresponse to antibiotic
B0051301biological_processcell division
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC1
Number of Residues5
Detailsbinding site for residue GOL A 601
ChainResidue
AGLU190
AGLY191
AARG298
AASN299
APRO397

site_idAC2
Number of Residues3
Detailsbinding site for residue SO4 A 602
ChainResidue
AARG67
AARG211
BARG408

site_idAC3
Number of Residues4
Detailsbinding site for residue SO4 A 603
ChainResidue
APRO289
AGLY290
AARG291
AARG288

site_idAC4
Number of Residues2
Detailsbinding site for residue SO4 A 604
ChainResidue
ASER294
AARG297

site_idAC5
Number of Residues3
Detailsbinding site for residue SO4 A 605
ChainResidue
AVAL390
AARG391
AHIS393

site_idAC6
Number of Residues2
Detailsbinding site for residue SO4 A 606
ChainResidue
AARG81
ALYS451

site_idAC7
Number of Residues7
Detailsbinding site for residue GOL B 601
ChainResidue
BGLU190
BGLY191
BARG297
BARG298
BASN299
BTHR303
BPRO397

site_idAC8
Number of Residues7
Detailsbinding site for residue GOL B 602
ChainResidue
BTYR284
BASP285
BARG288
BARG291
BALA292
BGLN296
BSO4608

site_idAC9
Number of Residues3
Detailsbinding site for residue SO4 B 603
ChainResidue
BSER342
BLYS361
BARG411

site_idAD1
Number of Residues2
Detailsbinding site for residue SO4 B 604
ChainResidue
AGLN457
BARG288

site_idAD2
Number of Residues3
Detailsbinding site for residue SO4 B 605
ChainResidue
BARG288
BPRO289
BGLY290

site_idAD3
Number of Residues2
Detailsbinding site for residue SO4 B 606
ChainResidue
BSER294
BARG297

site_idAD4
Number of Residues5
Detailsbinding site for residue SO4 B 607
ChainResidue
AGLU59
AGLN60
BARG345
BASN406
BARG409

site_idAD5
Number of Residues3
Detailsbinding site for residue SO4 B 608
ChainResidue
APRO446
BARG291
BGOL602

site_idAD6
Number of Residues3
Detailsbinding site for residue SO4 B 609
ChainResidue
BASP293
BSER294
BARG297

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|HAMAP-Rule:MF_02080
ChainResidueDetails
ASER310
BSER310

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PDB entries from 2024-10-09

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