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1LRU

Crystal Structure of E.coli Peptide Deformylase Complexed with Antibiotic Actinonin

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 Residues4
DetailsBINDING SITE FOR RESIDUE ZN A 601
ChainResidue
ACYS90
AHIS132
AHIS136
ABB2501

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN B 602
ChainResidue
BGLN50
BCYS90
BHIS132
BHIS136
BBB2502

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE ZN C 603
ChainResidue
CGLN50
CCYS90
CHIS132
CHIS136
CBB2503

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 701
ChainResidue
BHIS54
BGLN55
CARG29

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 702
ChainResidue
BARG29
CHIS54
CGLN55
CHOH746

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE BB2 A 501
ChainResidue
AGLY43
AILE44
AGLY45
AGLN50
AGLU87
AGLY89
ACYS90
ALEU91
AARG97
ALEU125
AHIS132
AGLU133
AHIS136
AZN601
AHOH684

site_idAC7
Number of Residues15
DetailsBINDING SITE FOR RESIDUE BB2 B 502
ChainResidue
BGLY43
BILE44
BGLY45
BGLN50
BGLU87
BGLU88
BGLY89
BCYS90
BLEU91
BARG97
BCYS129
BHIS132
BGLU133
BHIS136
BZN602

site_idAC8
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BB2 C 503
ChainResidue
CGLY43
CILE44
CGLY45
CGLN50
CGLU87
CGLU88
CGLY89
CCYS90
CLEU91
CARG97
CHIS132
CGLU133
CHIS136
CZN603

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:9846875
ChainResidueDetails
AMET134
BMET134
CMET134

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:9846875
ChainResidueDetails
ALEU91
AGLU133
ALEU137
BLEU91
BGLU133
BLEU137
CLEU91
CGLU133
CLEU137

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bs4
ChainResidueDetails
AGLU133
AGLY45
ALEU91
AGLN50

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bs4
ChainResidueDetails
BGLU133
BGLY45
BLEU91
BGLN50

site_idCSA3
Number of Residues4
DetailsAnnotated By Reference To The Literature 1bs4
ChainResidueDetails
CGLU133
CGLY45
CLEU91
CGLN50

site_idMCSA1
Number of Residues7
DetailsM-CSA 98
ChainResidueDetails
ALEU46activator, hydrogen bond acceptor
AVAL51electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
ALEU91metal ligand
ASER92electrostatic stabiliser, hydrogen bond donor
AGLU133metal ligand
AMET134hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
ALEU137metal ligand

site_idMCSA2
Number of Residues7
DetailsM-CSA 98
ChainResidueDetails
BLEU46activator, hydrogen bond acceptor
BVAL51electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BLEU91metal ligand
BSER92electrostatic stabiliser, hydrogen bond donor
BGLU133metal ligand
BMET134hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BLEU137metal ligand

site_idMCSA3
Number of Residues7
DetailsM-CSA 98
ChainResidueDetails
CLEU46activator, hydrogen bond acceptor
CVAL51electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
CLEU91metal ligand
CSER92electrostatic stabiliser, hydrogen bond donor
CGLU133metal ligand
CMET134hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CLEU137metal ligand

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PDB entries from 2024-07-24

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