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2RL3

Crystal structure of the OXA-10 W154H mutant at pH 7

Functional Information from GO Data
ChainGOidnamespacecontents
A0005886cellular_componentplasma membrane
A0008658molecular_functionpenicillin binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
A0071555biological_processcell wall organization
B0005886cellular_componentplasma membrane
B0008658molecular_functionpenicillin binding
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
B0071555biological_processcell wall organization
Functional Information from PDB Data
site_idAC2
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 1
ChainResidue
AGOL8
AHOH364
ASER67
ASER115
ALYS205
ATHR206
AGLY207
APHE208
AARG250
AHOH300

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 4
ChainResidue
ALYS134
ALYS138
ALYS152

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 11
ChainResidue
AARG250
AHOH346
AHOH454

site_idAC5
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 2
ChainResidue
BSER115
BTHR206
BGLY207
BPHE208
BARG250
BHOH372
BHOH396

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 3
ChainResidue
BTHR80
BARG131
BLYS134
BTYR135

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE EDO A 12
ChainResidue
AARG160
AHOH446

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 7
ChainResidue
AGOL9
AMET99
ALYS100
ASER147
AGLY148
AGLY149
AHOH277

site_idAC9
Number of Residues8
DetailsBINDING SITE FOR RESIDUE GOL A 8
ChainResidue
ASO41
ASER67
ATRP102
ASER115
AVAL117
AGLU129
APHE208
AHOH300

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 9
ChainResidue
AGOL7
AALA98
AMET99
AGLU129
AILE146
AGLY149
AILE150

site_idBC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE GOL A 13
ChainResidue
ALYS138
APHE139
ASER140
AGLU168
ASER172
AHOH283
AHOH434

site_idBC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE GOL B 5
ChainResidue
APRO198
AGLU199
AGLU227
AGLU229
AHOH343
BTHR107
BARG109
BGLY110
BHOH330

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE GOL B 6
ChainResidue
BLEU43
BSER50
BTYR233

site_idBC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE GOL B 10
ChainResidue
BLEU247
BPRO248
BARG250
BLYS251
BHOH355

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

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000269|PubMed:11724923, ECO:0000269|PubMed:19860471, ECO:0007744|PDB:1K54, ECO:0007744|PDB:2WGI
ChainResidueDetails
ASER67
BSER67

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:19860471, ECO:0007744|PDB:2WGI
ChainResidueDetails
ASER115
ATHR206
APHE208
AARG250
BSER115
BTHR206
BPHE208
BARG250

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-carboxylysine => ECO:0000269|PubMed:11188693, ECO:0000269|PubMed:11724923, ECO:0000269|PubMed:19860471, ECO:0007744|PDB:1E4D, ECO:0007744|PDB:1K4E, ECO:0007744|PDB:1K4F, ECO:0007744|PDB:1K54, ECO:0007744|PDB:1K55, ECO:0007744|PDB:1K56, ECO:0007744|PDB:1K57, ECO:0007744|PDB:1K6S, ECO:0007744|PDB:2RL3
ChainResidueDetails
AKCX70
BLYS70

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1m6k
ChainResidueDetails
ASER67

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1m6k
ChainResidueDetails
BSER67

237423

PDB entries from 2025-06-11

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