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5E2F

Crystal Structure of Beta-lactamase class D from Bacillus subtilis

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
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 301
ChainResidue
AASP41
AGLU42
AASP135
AHOH462
AHOH508
AHOH616

site_idAC2
Number of Residues4
Detailsbinding site for residue CA A 302
ChainResidue
AHOH599
AASP45
AHOH451
AHOH581

site_idAC3
Number of Residues5
Detailsbinding site for residue EDO A 303
ChainResidue
ASER124
ATHR215
AGLY216
ATHR217
AHOH403

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 304
ChainResidue
AARG71
AGLY151
AHOH432
BARG71
BHOH496

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 300
ChainResidue
BASP47
BHOH426
BHOH525
BHOH606
BHOH613
BHOH631

site_idAC6
Number of Residues2
Detailsbinding site for residue EDO B 301
ChainResidue
BASN64
BHOH497

Functional Information from PROSITE/UniProt
site_idPS00337
Number of Residues11
DetailsBETA_LACTAMASE_D Beta-lactamase class-D active site. PqSTFKVVnAL
ChainResidueDetails
APRO74-LEU84

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Acyl-ester intermediate","evidences":[{"source":"PROSITE-ProRule","id":"PRU10103","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues4
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsModified residue: {"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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