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1ZZ8

Crystal Structure of FeII HppE in Complex with Substrate Form 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0008198molecular_functionferrous iron binding
A0016491molecular_functionoxidoreductase activity
A0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
A0017000biological_processantibiotic biosynthetic process
A0046872molecular_functionmetal ion binding
A0051213molecular_functiondioxygenase activity
A0051289biological_processprotein homotetramerization
A0055114biological_processobsolete oxidation-reduction process
A1901766biological_processphosphinothricin biosynthetic process
B0003677molecular_functionDNA binding
B0008198molecular_functionferrous iron binding
B0016491molecular_functionoxidoreductase activity
B0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
B0017000biological_processantibiotic biosynthetic process
B0046872molecular_functionmetal ion binding
B0051213molecular_functiondioxygenase activity
B0051289biological_processprotein homotetramerization
B0055114biological_processobsolete oxidation-reduction process
B1901766biological_processphosphinothricin biosynthetic process
C0003677molecular_functionDNA binding
C0008198molecular_functionferrous iron binding
C0016491molecular_functionoxidoreductase activity
C0016717molecular_functionoxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
C0017000biological_processantibiotic biosynthetic process
C0046872molecular_functionmetal ion binding
C0051213molecular_functiondioxygenase activity
C0051289biological_processprotein homotetramerization
C0055114biological_processobsolete oxidation-reduction process
C1901766biological_processphosphinothricin biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 A 199
ChainResidue
AHIS138
AGLU142
AHIS180
AS0H1001
AHOH1039

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE FE2 B 199
ChainResidue
BHIS138
BGLU142
BHIS180
BS0H1003

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE FE2 C 199
ChainResidue
CHIS138
CGLU142
CHIS180
CS0H1002
CHOH1060

site_idAC4
Number of Residues10
DetailsBINDING SITE FOR RESIDUE S0H A 1001
ChainResidue
AARG97
ATYR103
ATYR105
AASN135
AHIS138
AGLU142
AFE2199
AHOH1003
BLYS23
BHOH1031

site_idAC5
Number of Residues11
DetailsBINDING SITE FOR RESIDUE S0H C 1002
ChainResidue
CLYS23
CARG97
CTYR103
CTYR105
CASN135
CHIS138
CGLU142
CHIS180
CFE2199
CHOH1058
CHOH1059

site_idAC6
Number of Residues9
DetailsBINDING SITE FOR RESIDUE S0H B 1003
ChainResidue
ALYS23
BARG97
BTYR105
BASN135
BHIS138
BGLU142
BHIS180
BFE2199
BHOH1006

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues57
DetailsDNA_BIND: H-T-H motif => ECO:0000255|PROSITE-ProRule:PRU00257
ChainResidueDetails
AHIS26-ASN45
BHIS26-ASN45
CHIS26-ASN45

site_idSWS_FT_FI2
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16186494, ECO:0000269|PubMed:21682308, ECO:0007744|PDB:2BNN, ECO:0007744|PDB:3SCH, ECO:0007744|PDB:4J1W, ECO:0007744|PDB:4J1X
ChainResidueDetails
ALYS23
BLYS23
CLYS23

site_idSWS_FT_FI3
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16015285, ECO:0000269|PubMed:16186494, ECO:0000269|PubMed:21682308, ECO:0007744|PDB:1ZZ8, ECO:0007744|PDB:2BNN, ECO:0007744|PDB:3SCG, ECO:0007744|PDB:3SCH, ECO:0007744|PDB:4J1W, ECO:0007744|PDB:4J1X
ChainResidueDetails
AARG97
BARG97
CARG97

site_idSWS_FT_FI4
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16015285, ECO:0000269|PubMed:16186494, ECO:0000269|PubMed:21682308, ECO:0007744|PDB:1ZZ8, ECO:0007744|PDB:1ZZB, ECO:0007744|PDB:2BNN, ECO:0007744|PDB:3SCF, ECO:0007744|PDB:3SCG, ECO:0007744|PDB:3SCH, ECO:0007744|PDB:4J1W, ECO:0007744|PDB:4J1X
ChainResidueDetails
ATYR105
BTYR105
CTYR105

site_idSWS_FT_FI5
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16015285, ECO:0000269|PubMed:16186494, ECO:0000269|PubMed:21682308, ECO:0007744|PDB:1ZZ7, ECO:0007744|PDB:1ZZ8, ECO:0007744|PDB:1ZZB, ECO:0007744|PDB:2BNN, ECO:0007744|PDB:3SCF, ECO:0007744|PDB:3SCG, ECO:0007744|PDB:3SCH, ECO:0007744|PDB:4J1W, ECO:0007744|PDB:4J1X
ChainResidueDetails
AASN135
BASN135
CASN135

site_idSWS_FT_FI6
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:16015285, ECO:0000269|PubMed:16186494, ECO:0000269|PubMed:21682308, ECO:0007744|PDB:1ZZ7, ECO:0007744|PDB:1ZZ8, ECO:0007744|PDB:1ZZ9, ECO:0007744|PDB:2BNM, ECO:0007744|PDB:2BNN, ECO:0007744|PDB:2BNO, ECO:0007744|PDB:3SCF, ECO:0007744|PDB:3SCG, ECO:0007744|PDB:4J1W, ECO:0007744|PDB:4J1X
ChainResidueDetails
AHIS138
AHIS180
BHIS138
BHIS180
CHIS138
CHIS180

site_idSWS_FT_FI7
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:16015285, ECO:0000269|PubMed:16186494, ECO:0000269|PubMed:21682308, ECO:0007744|PDB:1ZZ7, ECO:0007744|PDB:1ZZ8, ECO:0007744|PDB:1ZZB, ECO:0007744|PDB:2BNN, ECO:0007744|PDB:3SCF, ECO:0007744|PDB:3SCG, ECO:0007744|PDB:3SCH, ECO:0007744|PDB:4J1W
ChainResidueDetails
AGLU142
BGLU142
CGLU142

218853

PDB entries from 2024-04-24

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