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1BS7

PEPTIDE DEFORMYLASE AS NI2+ CONTAINING FORM

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 SO4 B 3001
ChainResidue
BASP552
BILE553
BHIS554
BGLN555
CARG1029

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 3002
ChainResidue
BARG529
CILE1053
CHIS1054
CGLN1055

site_idAC3
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NI A 2001
ChainResidue
ACYS90
AHIS132
AHIS136
AHOH2034

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI B 2001
ChainResidue
BGLN550
BCYS590
BHIS632
BHIS636
BHOH3004

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NI C 2001
ChainResidue
CGLN1050
CCYS1090
CHIS1132
CHIS1136
CHOH3005

site_idNIA
Number of Residues3
DetailsNI BINDING SITE FOR CHAIN A
ChainResidue
ACYS90
AHIS132
AHIS136

site_idNIB
Number of Residues3
DetailsNI BINDING SITE FOR CHAIN B
ChainResidue
BCYS590
BHIS632
BHIS636

site_idNIC
Number of Residues3
DetailsNI BINDING SITE FOR CHAIN C
ChainResidue
CCYS1090
CHIS1132
CHIS1136

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues3
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:9846875
ChainResidueDetails
AMET134
BMET634
CMET1134

site_idSWS_FT_FI2
Number of Residues9
DetailsBINDING: BINDING => ECO:0000269|PubMed:9846875
ChainResidueDetails
ALEU91
AGLU133
ALEU137
BLEU591
BGLU633
BLEU637
CLEU1091
CGLU1133
CLEU1137

Catalytic Information from CSA
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
BLEU546activator, hydrogen bond acceptor
BVAL551electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
BLEU591metal ligand
BSER592electrostatic stabiliser, hydrogen bond donor
BGLU633metal ligand
BMET634hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
BLEU637metal ligand

site_idMCSA3
Number of Residues7
DetailsM-CSA 98
ChainResidueDetails
CLEU1046activator, hydrogen bond acceptor
CVAL1051electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor
CLEU1091metal ligand
CSER1092electrostatic stabiliser, hydrogen bond donor
CGLU1133metal ligand
CMET1134hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
CLEU1137metal ligand

217705

PDB entries from 2024-03-27

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