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1PI5

Structure of N289A mutant of AmpC in complex with SM2, carboxyphenylglycylboronic acid bearing the cephalothin R1 side chain

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0030288cellular_componentouter membrane-bounded periplasmic space
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0030288cellular_componentouter membrane-bounded periplasmic space
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 1
ChainResidue
AARG133
AHIS186
AHOH490
AHOH502
AHOH729
AHOH933
BLYS290
BHOH790

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE K A 2
ChainResidue
AASP217
AHOH522
AHOH569
AHOH832
AGLY214

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE K B 3
ChainResidue
BGLY214
BASP217
BHOH486
BHOH488
BHOH536
BHOH611

site_idAC4
Number of Residues11
DetailsBINDING SITE FOR RESIDUE SM2 A 401
ChainResidue
ASER64
ALEU119
ATYR150
AASN152
ATYR221
AGLY317
AALA318
ATHR319
AGLY320
AHOH791
AHOH840

site_idAC5
Number of Residues12
DetailsBINDING SITE FOR RESIDUE SM2 B 400
ChainResidue
ATRP93
ASER128
AHOH703
BASN279
BSER282
BASN285
BGLY286
BILE291
BARG296
BHOH781
BHOH782
BHOH953

site_idAC6
Number of Residues17
DetailsBINDING SITE FOR RESIDUE SM2 B 401
ChainResidue
BSER64
BLEU119
BGLN120
BTYR150
BASN152
BTYR221
BGLY317
BALA318
BTHR319
BGLY320
BASN343
BHOH498
BHOH607
BHOH660
BHOH824
BHOH889
BHOH965

Functional Information from PROSITE/UniProt
site_idPS00336
Number of Residues8
DetailsBETA_LACTAMASE_C Beta-lactamase class-C active site. FELGSVSK
ChainResidueDetails
APHE60-LYS67

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Acyl-ester intermediate => ECO:0000255|PROSITE-ProRule:PRU10102, ECO:0000269|PubMed:11478888, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY
ChainResidueDetails
ASER64
AASN152
AALA318
BSER64
BTYR150
BASN152
BALA318
ATYR150

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PDB entries from 2024-06-12

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