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1G2A

THE CRYSTAL STRUCTURE OF E.COLI PEPTIDE DEFORMYLASE COMPLEXED WITH 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 Residues5
DetailsBINDING SITE FOR RESIDUE NI A 1169
ChainResidue
AGLN50
ACYS90
AHIS132
AHIS136
ABB21001

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI B 2169
ChainResidue
BBB22002
BGLN50
BCYS90
BHIS132
BHIS136

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI C 3169
ChainResidue
CGLN50
CCYS90
CHIS132
CHIS136
CBB23003

site_idAC4
Number of Residues14
DetailsBINDING SITE FOR RESIDUE BB2 A 1001
ChainResidue
AGLU42
AGLY43
AILE44
AGLY45
AGLN50
AGLU87
AGLY89
ACYS90
ALEU91
AARG97
AHIS132
AGLU133
AHIS136
ANI1169

site_idAC5
Number of Residues15
DetailsBINDING SITE FOR RESIDUE BB2 B 2002
ChainResidue
BGLU42
BGLY43
BILE44
BGLY45
BGLN50
BGLU87
BGLU88
BGLY89
BCYS90
BLEU91
BARG97
BHIS132
BGLU133
BHIS136
BNI2169

site_idAC6
Number of Residues15
DetailsBINDING SITE FOR RESIDUE BB2 C 3003
ChainResidue
CGLY43
CILE44
CGLY45
CGLN50
CGLU87
CGLY89
CCYS90
CLEU91
CARG97
CHIS132
CGLU133
CHIS136
CNI3169
CHOH3184
CHOH3226

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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