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3N2W

Crystal structure of the N-terminal beta-aminopeptidase BapA from Sphingosinicella xenopeptidilytica

Functional Information from GO Data
ChainGOidnamespacecontents
A0004177molecular_functionaminopeptidase activity
A0006508biological_processproteolysis
A0042597cellular_componentperiplasmic space
A0042802molecular_functionidentical protein binding
B0004177molecular_functionaminopeptidase activity
B0006508biological_processproteolysis
B0042597cellular_componentperiplasmic space
B0042802molecular_functionidentical protein binding
C0004177molecular_functionaminopeptidase activity
C0006508biological_processproteolysis
C0042597cellular_componentperiplasmic space
C0042802molecular_functionidentical protein binding
D0004177molecular_functionaminopeptidase activity
D0006508biological_processproteolysis
D0042597cellular_componentperiplasmic space
D0042802molecular_functionidentical protein binding
Functional Information from PDB Data
site_idAC1
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL A 374
ChainResidue
AVAL88
DASN314
DASP315
AGLY89
AGLN90
APRO263
AHIS299
AILE301
APRO307
DMET262
DHIS264

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL A 375
ChainResidue
APHE124
ASER125
AARG126
ALEU127

site_idAC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 376
ChainResidue
AGLY285
AALA286
ALEU287
ASER288
AHOH501
AHOH1067
CSER318
CASN322

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 A 377
ChainResidue
AGLU224
AILE365
AALA368
AARG369
AHOH1345
AHOH1403

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL B 374
ChainResidue
BVAL88
BGLY89
BGLN90
BPRO263
BHIS299
BILE301
BPRO307
CMET262
CHIS264
CASN314
CASP315

site_idAC6
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL C 374
ChainResidue
BMET262
BHIS264
BASN314
BASP315
CVAL88
CGLY89
CGLN90
CPRO263
CHIS299
CILE301
CPRO307

site_idAC7
Number of Residues10
DetailsBINDING SITE FOR RESIDUE GOL C 375
ChainResidue
CTHR76
CGLY77
CGLU133
CTHR134
CLEU135
CSER250
CLEU287
CSO4379
CHOH453
DLEU128

site_idAC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL C 376
ChainResidue
CLEU84
CPHE124
CSER125
CLEU127

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 377
ChainResidue
ASER318
AASN322
CGLY285
CALA286
CLEU287
CSER288
CHOH421
CHOH1093

site_idBC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 C 378
ChainResidue
BLYS306
CILE312
CILE313
CASN314
CASP317
CHOH771

site_idBC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 C 379
ChainResidue
CLEU135
CASN207
CSER250
CLEU287
CSER288
CGOL375
CHOH719
CHOH1093

site_idBC3
Number of Residues11
DetailsBINDING SITE FOR RESIDUE GOL D 374
ChainResidue
AMET262
AHIS264
AASN314
AASP315
DVAL88
DGLY89
DGLN90
DPRO263
DHIS299
DILE301
DPRO307

site_idBC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL D 375
ChainResidue
DSER125
DARG126
DLEU127
DPHE124

site_idBC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 D 376
ChainResidue
BSER318
BASN322
DGLY285
DALA286
DLEU287
DSER288
DHOH489

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 D 377
ChainResidue
DGLY13
DTHR14
DHOH407
DHOH454
DHOH513

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 2024-07-24

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