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4WZ5

Crystal structure of P. aeruginosa OXA10

Functional Information from GO Data
ChainGOidnamespacecontents
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
C0008658molecular_functionpenicillin binding
C0008800molecular_functionbeta-lactamase activity
C0017001biological_processantibiotic catabolic process
D0008658molecular_functionpenicillin binding
D0008800molecular_functionbeta-lactamase activity
D0017001biological_processantibiotic catabolic process
Functional Information from PDB Data
site_idAC1
Number of Residues1
Detailsbinding site for residue SO4 A 301
ChainResidue
AARG160

site_idAC2
Number of Residues4
Detailsbinding site for residue SO4 A 302
ChainResidue
ATHR80
AARG131
ALYS134
ATYR135

site_idAC3
Number of Residues13
Detailsbinding site for residue 3VU A 303
ChainResidue
AVAL117
ALEU155
AGLY207
APHE208
ASER209
AARG250
AHOH416
AHOH430
AHOH459
AALA66
ASER67
ATRP102
ASER115

site_idAC4
Number of Residues4
Detailsbinding site for residue SO4 B 301
ChainResidue
BTHR80
BARG131
BLYS134
BTYR135

site_idAC5
Number of Residues2
Detailsbinding site for residue SO4 B 302
ChainResidue
BARG160
BHOH470

site_idAC6
Number of Residues4
Detailsbinding site for residue SO4 B 303
ChainResidue
BGLY128
BGLU129
BVAL130
BHOH448

site_idAC7
Number of Residues14
Detailsbinding site for residue 3VU B 304
ChainResidue
BALA66
BSER67
BTRP102
BSER115
BVAL117
BLEU155
BGLY207
BPHE208
BSER209
BARG250
BHOH418
BHOH436
BHOH439
BHOH451

site_idAC8
Number of Residues9
Detailsbinding site for residue SO4 C 301
ChainResidue
BLYS95
CSER67
CSER115
CLYS205
CTHR206
CGLY207
CPHE208
CARG250
CHOH452

site_idAC9
Number of Residues4
Detailsbinding site for residue SO4 C 302
ChainResidue
CTYR63
CLEU64
CVAL219
CHOH472

site_idAD1
Number of Residues3
Detailsbinding site for residue SO4 C 303
ChainResidue
CSER181
CLYS182
CHOH457

site_idAD2
Number of Residues7
Detailsbinding site for residue SO4 C 304
ChainResidue
ATHR107
AARG109
CPRO198
CGLU227
CGLU229
CHOH440
CHOH464

site_idAD3
Number of Residues6
Detailsbinding site for residue CO2 C 305
ChainResidue
CSER67
CLYS70
CVAL117
CPHE120
CTRP154
CLEU155

site_idAD4
Number of Residues9
Detailsbinding site for residue SO4 D 301
ChainResidue
ALYS95
DSER67
DSER115
DLYS205
DTHR206
DGLY207
DPHE208
DARG250
DHOH543

site_idAD5
Number of Residues9
Detailsbinding site for residue SO4 D 302
ChainResidue
BGLU199
BTYR200
BGLU227
BGLU229
DTHR107
DARG109
DGLY110
DHOH460
DHOH530

site_idAD6
Number of Residues8
Detailsbinding site for residue SO4 D 303
ChainResidue
BTHR107
BARG109
DPRO198
DGLU199
DTYR200
DGLU227
DGLU229
DHOH448

site_idAD7
Number of Residues3
Detailsbinding site for residue SO4 D 304
ChainResidue
DLYS182
BHOH477
DSER181

site_idAD8
Number of Residues7
Detailsbinding site for residue CO2 D 305
ChainResidue
DSER67
DLYS70
DVAL117
DPHE120
DTRP154
DLEU155
DHOH442

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PaSTFKIPnAI
ChainResidueDetails
APRO65-ILE75
CPRO65-ILE75

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate
ChainResidueDetails
CSER67
DSER67

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250
ChainResidueDetails
CLYS205
DLYS205

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:11188693
ChainResidueDetails
CLYS70
DLYS70

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PDB entries from 2024-07-17

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