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5F1F

Crystal structure of CMY-10 adenylylated by acetyl-AMP

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0046677biological_processresponse to antibiotic
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CD A 401
ChainResidue
AHIS161
AHOH540
AHOH727
AHOH731
AHOH750
AHOH754

site_idAC2
Number of Residues5
Detailsbinding site for residue CD A 402
ChainResidue
AHOH752
AHOH758
AGLU207
AVAL278
AHIS351

site_idAC3
Number of Residues4
Detailsbinding site for residue CD A 403
ChainResidue
AHIS24
AGLY359
AHOH762
AHOH767

site_idAC4
Number of Residues6
Detailsbinding site for residue CD A 404
ChainResidue
AASP244
AHIS259
AHOH566
AHOH715
AHOH748
AHOH763

site_idAC5
Number of Residues5
Detailsbinding site for residue CD A 405
ChainResidue
AASP14
AGLU294
AHOH508
AHOH721
AHOH755

site_idAC6
Number of Residues5
Detailsbinding site for residue CD A 406
ChainResidue
AHIS0
AGLU50
AHIS148
AHOH568
AHOH708

site_idAC7
Number of Residues12
Detailsbinding site for residue AMP A 407
ChainResidue
ASER65
AGLN121
ATYR151
AASN153
ATYR223
AGLY314
ASER315
ATHR316
AHOH525
AHOH581
AHOH609
AHOH682

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FEIGSVSK
ChainResidueDetails
APHE61-LYS68

224201

PDB entries from 2024-08-28

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