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3FKW

AmpC K67R mutant apo structure

Functional Information from GO Data
ChainGOidnamespacecontents
A0008800molecular_functionbeta-lactamase activity
A0016787molecular_functionhydrolase activity
A0017001biological_processantibiotic catabolic process
A0042597cellular_componentperiplasmic space
A0046677biological_processresponse to antibiotic
B0008800molecular_functionbeta-lactamase activity
B0016787molecular_functionhydrolase activity
B0017001biological_processantibiotic catabolic process
B0042597cellular_componentperiplasmic space
B0046677biological_processresponse to antibiotic
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE PO4 A 502
ChainResidue
ASER64
ATYR150
AGLY317
AALA318
AHOH1295
AHOH1759
AHOH1929

site_idAC2
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 A 503
ChainResidue
AHOH1105
AHOH1510
AHOH1526
AHOH1529
AHOH1591
AHOH1848
BLYS290
AARG133
AHIS186

site_idAC3
Number of Residues9
DetailsBINDING SITE FOR RESIDUE PO4 B 501
ChainResidue
BSER64
BTYR150
BGLY317
BALA318
BHOH1319
BHOH1445
BHOH1561
BHOH1732
BHOH1831

site_idAC4
Number of Residues2
DetailsBINDING SITE FOR RESIDUE K B 504
ChainResidue
AHOH1232
BHOH1420

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:12005439, ECO:0000269|PubMed:16506777, ECO:0000269|PubMed:35486701, ECO:0000269|PubMed:6795623, ECO:0000269|PubMed:9819201, ECO:0000269|DOI:10.1021/ja001676x
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:2FFY
ChainResidueDetails
ASER64
BSER64

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9
ChainResidueDetails
AGLN120
BGLN120

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:16506777, ECO:0007744|PDB:2FFY
ChainResidueDetails
ATYR150
BTYR150

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0000269|PubMed:12323371, ECO:0000269|PubMed:16506777, ECO:0000269|DOI:10.1021/ja001676x, ECO:0007744|PDB:1FCN, ECO:0007744|PDB:1KVM, ECO:0007744|PDB:1LL9, ECO:0007744|PDB:2FFY
ChainResidueDetails
AASN152
AALA318
BASN152
BALA318

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12005439, ECO:0007744|PDB:1KVM
ChainResidueDetails
AASN343
BASN343

Catalytic Information from CSA
site_idCSA1
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
AGLU272
ASER64
ALYS315
ATYR150
AARG67

site_idCSA2
Number of Residues5
DetailsAnnotated By Reference To The Literature 1xx2
ChainResidueDetails
BGLU272
BSER64
BLYS315
BTYR150
BARG67

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PDB entries from 2024-10-09

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