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3K6L

The structure of E.coli peptide deformylase (PDF) in complex with peptidomimetic ligand BB2827

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0008198molecular_functionferrous iron binding
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0042586molecular_functionpeptide deformylase activity
A0043022molecular_functionribosome binding
A0043686biological_processco-translational protein modification
A0046872molecular_functionmetal ion binding
B0005515molecular_functionprotein binding
B0005829cellular_componentcytosol
B0006412biological_processtranslation
B0008198molecular_functionferrous iron binding
B0008270molecular_functionzinc ion binding
B0016787molecular_functionhydrolase activity
B0042586molecular_functionpeptide deformylase activity
B0043022molecular_functionribosome binding
B0043686biological_processco-translational protein modification
B0046872molecular_functionmetal ion binding
C0005515molecular_functionprotein binding
C0005829cellular_componentcytosol
C0006412biological_processtranslation
C0008198molecular_functionferrous iron binding
C0008270molecular_functionzinc ion binding
C0016787molecular_functionhydrolase activity
C0042586molecular_functionpeptide deformylase activity
C0043022molecular_functionribosome binding
C0043686biological_processco-translational protein modification
C0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI A 169
ChainResidue
AGLN50
ACYS90
AHIS132
AHIS136
A2BB170

site_idAC2
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 2BB A 170
ChainResidue
AGLN50
AILE86
AGLY89
ACYS90
ALEU91
AARG97
ACYS129
AHIS132
AGLU133
AHIS136
ANI169
AHOH249
AHOH264
AGLU42
AGLY43
AILE44
AGLY45

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI B 169
ChainResidue
BGLN50
BCYS90
BHIS132
BHIS136
B2BB170

site_idAC4
Number of Residues16
DetailsBINDING SITE FOR RESIDUE 2BB B 170
ChainResidue
BGLU42
BGLY43
BILE44
BGLY45
BGLN50
BILE86
BGLU88
BGLY89
BCYS90
BLEU91
BCYS129
BHIS132
BGLU133
BHIS136
BNI169
BHOH263

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI C 169
ChainResidue
CGLN50
CCYS90
CHIS132
CHIS136
CHOH208

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:9846875
ChainResidueDetails
AGLU133
BGLU133
CGLU133

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:9846875
ChainResidueDetails
ACYS90
AHIS132
AHIS136
BCYS90
BHIS132
BHIS136
CCYS90
CHIS132
CHIS136

Catalytic Information from CSA
site_idMCSA1
Number of Residues7
DetailsM-CSA 98
ChainResidueDetails
AGLY45activator, hydrogen bond acceptor
AGLN50electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
ACYS90metal ligand
ALEU91electrostatic stabiliser, hydrogen bond donor
AHIS132metal ligand
AGLU133hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
AHIS136metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 98
ChainResidueDetails
BGLY45activator, hydrogen bond acceptor
BGLN50electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BCYS90metal ligand
BLEU91electrostatic stabiliser, hydrogen bond donor
BHIS132metal ligand
BGLU133hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BHIS136metal ligand

site_idMCSA3
Number of Residues7
DetailsM-CSA 98
ChainResidueDetails
CGLY45activator, hydrogen bond acceptor
CGLN50electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
CCYS90metal ligand
CLEU91electrostatic stabiliser, hydrogen bond donor
CHIS132metal ligand
CGLU133hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CHIS136metal ligand

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PDB entries from 2024-04-24

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