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1BSJ

COBALT DEFORMYLASE INHIBITOR COMPLEX FROM E.COLI

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005829cellular_componentcytosol
A0006412biological_processtranslation
A0008198molecular_functionferrous iron binding
A0008270molecular_functionzinc ion binding
A0016787molecular_functionhydrolase activity
A0031365biological_processN-terminal protein amino acid modification
A0042586molecular_functionpeptide deformylase activity
A0043022molecular_functionribosome binding
A0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CO A 169
ChainResidue
AGLN50
ACYS90
AHIS132
AHIS136
AMLN171

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE PO4 A 170
ChainResidue
AGLN152
AARG155
AGLN156
AGLU159
APRO9
AASP10
AGLU11
AARG14

site_idAC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE MLN A 171
ChainResidue
AGLU42
AGLY43
AILE44
AGLY45
AGLN50
AILE86
AILE86
AGLY89
ACYS90
ALEU91
AGLY124
ALEU125
AILE128
AHIS132
AGLU133
AHIS136
ACO169

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"9846875","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"9846875","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues4
Detailsa catalytic site defined by CSA, PubMed 9846875
ChainResidueDetails
AGLU133
AGLY45
ALEU91
AGLN50

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

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PDB entries from 2025-12-24

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