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3I92

Structure of the cytosolic domain of E. coli FeoB, GppCH2p-bound form

Functional Information from GO Data
ChainGOidnamespacecontents
A0005525molecular_functionGTP binding
A0006826biological_processiron ion transport
A0015093molecular_functionferrous iron transmembrane transporter activity
A0016020cellular_componentmembrane
B0005525molecular_functionGTP binding
B0006826biological_processiron ion transport
B0015093molecular_functionferrous iron transmembrane transporter activity
B0016020cellular_componentmembrane
C0005525molecular_functionGTP binding
C0006826biological_processiron ion transport
C0015093molecular_functionferrous iron transmembrane transporter activity
C0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG A 801
ChainResidue
ALYS16
ATHR17
AGCP800

site_idAC2
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GCP A 800
ChainResidue
AASN120
AMET121
AASP123
AVAL149
ATHR151
AMG801
AASN13
ASER14
AGLY15
ALYS16
ATHR17
ATHR18

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG B 803
ChainResidue
BLYS16
BTHR17
BGCP802

site_idAC4
Number of Residues15
DetailsBINDING SITE FOR RESIDUE GCP B 802
ChainResidue
BPRO12
BASN13
BSER14
BGLY15
BLYS16
BTHR17
BTHR18
BASN120
BMET121
BASP123
BILE124
BVAL149
BSER150
BTHR151
BMG803

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE MG C 805
ChainResidue
CLYS16
CTHR17
CGCP804

site_idAC6
Number of Residues12
DetailsBINDING SITE FOR RESIDUE GCP C 804
ChainResidue
CPRO12
CASN13
CSER14
CGLY15
CLYS16
CTHR17
CTHR18
CASN120
CMET121
CASP123
CILE124
CMG805

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01048","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19629046","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues21
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01048","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues9
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01048","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19629046","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"12446835","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU01048","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19629046","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25374115","evidenceCode":"ECO:0000269"},{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues332
DetailsDomain: {"description":"FeoB-type G","evidences":[{"source":"PROSITE-ProRule","id":"PRU01048","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
ATHR60

site_idCSA2
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
BTHR60

site_idCSA3
Number of Residues1
DetailsAnnotated By Reference To The Literature 1ksj
ChainResidueDetails
CTHR60

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PDB entries from 2026-01-14

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