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1FOF

CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-10

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_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 490
ChainResidue
AHIS203
AGLU227
BGLU190
BHOH547
BHOH575

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO B 491
ChainResidue
BGLU227
AGLU190
AHOH648
AHOH649
BHIS203

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE SO4 A 488
ChainResidue
ASER67
ASER115
ALYS205
ATHR206
AGLY207
APHE208
AARG250
AHOH491
AHOH617
AHOH749

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 B 489
ChainResidue
BSER67
BSER115
BTHR206
BGLY207
BPHE208
BARG250
BHOH534

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
ALYS70
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

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PDB entries from 2025-06-18

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