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7MQN

Crystal structure of class C beta lactamase from Rhodobacter sphaeroides

Functional Information from GO Data
ChainGOidnamespacecontents
A0006508biological_processproteolysis
A0008233molecular_functionpeptidase activity
A0008800molecular_functionbeta-lactamase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046677biological_processresponse to antibiotic
B0006508biological_processproteolysis
B0008233molecular_functionpeptidase activity
B0008800molecular_functionbeta-lactamase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues8
Detailsbinding site for residue PO4 A 401
ChainResidue
ASER84
ATYR168
ALYS332
ATHR333
AGLY334
APO4403
AHOH502
AHOH511

site_idAC2
Number of Residues7
Detailsbinding site for residue PO4 A 402
ChainResidue
ATYR188
AALA189
AASP238
AGLU239
AHOH528
AHOH621
ASER187

site_idAC3
Number of Residues7
Detailsbinding site for residue PO4 A 403
ChainResidue
ATYR308
ASER335
AASN363
AARG366
APO4401
AHOH510
AHOH608

site_idAC4
Number of Residues9
Detailsbinding site for residue PO4 B 401
ChainResidue
BSER84
BTYR168
BLYS332
BTHR333
BGLY334
BPO4402
BHOH509
BHOH511
BHOH657

site_idAC5
Number of Residues5
Detailsbinding site for residue PO4 B 402
ChainResidue
BTYR308
BSER335
BASN363
BPO4401
BHOH619

site_idAC6
Number of Residues8
Detailsbinding site for residue PO4 B 403
ChainResidue
BTYR188
BALA189
BASP238
BGLU239
BHOH540
BHOH548
BHOH553
BHOH598

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSISK
ChainResidueDetails
APHE80-LYS87

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PDB entries from 2024-07-24

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