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3NFB

Crystal structure of the N-terminal beta-aminopeptidase BapA in complex with hydrolyzed ampicillin

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0016787molecular_functionhydrolase activity
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
B0004177molecular_functionaminopeptidase activity
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0016787molecular_functionhydrolase activity
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
C0004177molecular_functionaminopeptidase activity
C0006508biological_processproteolysis
C0008233molecular_functionpeptidase activity
C0016787molecular_functionhydrolase activity
C0042597cellular_componentperiplasmic space
C0042802molecular_functionidentical protein binding
D0004177molecular_functionaminopeptidase activity
D0006508biological_processproteolysis
D0008233molecular_functionpeptidase activity
D0016787molecular_functionhydrolase activity
D0042597cellular_componentperiplasmic space
D0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL A 374
ChainResidue
AVAL88
BASP315
AGLY89
AGLN90
APRO263
AHIS299
AILE301
APRO307
BMET262
BHIS264

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL A 375
ChainResidue
AMET262
AHIS264
AASP315
BVAL88
BGLN90
BPRO263
BHIS299
BILE301
BPRO307

site_idAC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE OAE A 376
ChainResidue
ATHR76
AGLU133
ALEU135
AASN207
ASER250
ALEU287
ASO4378
AHOH406
AHOH690
AHOH1079
CPHE124

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE OAE A 377
ChainResidue
AARG138
AVAL232
AALA237
AALA238
AHOH896
AHOH1065
AHOH1079

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 378
ChainResidue
AALA286
ALEU287
ASER288
AOAE376
AHOH696
DSER318
DASN322

site_idAC6
Number of Residues13
DetailsBINDING SITE FOR RESIDUE OAE B 374
ChainResidue
BTHR76
BGLY77
BGLU133
BLEU135
BASN137
BASN207
BSER250
BLEU287
BHOH386
BHOH734
CSO4377
CHOH989
DPHE124

site_idAC7
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 B 375
ChainResidue
BSER318
BASN322
BHOH746
CGLY285
CALA286
CLEU287
CSER288
COAE376

site_idAC8
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL C 374
ChainResidue
CMET262
CHIS264
CASP315
DVAL88
DGLY89
DGLN90
DPRO263
DHIS299
DILE301
DPRO307

site_idAC9
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL C 375
ChainResidue
CVAL88
CGLY89
CGLN90
CPRO263
CHIS299
CILE301
CPRO307
DHIS264
DASP315

site_idBC1
Number of Residues12
DetailsBINDING SITE FOR RESIDUE OAE C 376
ChainResidue
APHE124
BSO4375
CTHR76
CGLY77
CGLU133
CLEU135
CASN207
CSER250
CLEU287
CHOH407
CHOH899
CHOH943

site_idBC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 C 377
ChainResidue
BSER288
BOAE374
CSER318
CASN322
CHOH653
CHOH989
BGLY285
BALA286
BLEU287

site_idBC3
Number of Residues15
DetailsBINDING SITE FOR RESIDUE OAE D 374
ChainResidue
BPHE124
DTHR76
DGLY77
DGLU133
DLEU135
DASN137
DASN207
DSER250
DLEU287
DSO4376
DHOH392
DHOH773
DHOH978
DHOH991
DHOH1120

site_idBC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE OAE D 375
ChainResidue
DARG138
DALA237
DALA238
DHOH709
DHOH978
DHOH1111

site_idBC5
Number of Residues9
DetailsBINDING SITE FOR RESIDUE SO4 D 376
ChainResidue
ASER318
AASN322
DGLY285
DALA286
DLEU287
DSER288
DOAE374
DHOH412
DHOH1120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile => ECO:0000303|PubMed:22980995
ChainResidueDetails
ASER250
BSER250
CSER250
DSER250

site_idSWS_FT_FI2
Number of Residues8
DetailsACT_SITE: Proton donor/acceptor => ECO:0000303|PubMed:22980995
ChainResidueDetails
ASER288
AGLU290
BSER288
BGLU290
CSER288
CGLU290
DSER288
DGLU290

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PDB entries from 2024-04-24

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