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2HYF

The Structure of apo-MntR from Bacillus subtilis, selenomethionine derivative

Functional Information from GO Data
ChainGOidnamespacecontents
A0003677molecular_functionDNA binding
A0003700molecular_functionDNA-binding transcription factor activity
A0005737cellular_componentcytoplasm
A0006355biological_processregulation of DNA-templated transcription
A0030026biological_processintracellular manganese ion homeostasis
A0030145molecular_functionmanganese ion binding
A0046872molecular_functionmetal ion binding
A0046914molecular_functiontransition metal ion binding
A0046983molecular_functionprotein dimerization activity
B0003677molecular_functionDNA binding
B0003700molecular_functionDNA-binding transcription factor activity
B0005737cellular_componentcytoplasm
B0006355biological_processregulation of DNA-templated transcription
B0030026biological_processintracellular manganese ion homeostasis
B0030145molecular_functionmanganese ion binding
B0046872molecular_functionmetal ion binding
B0046914molecular_functiontransition metal ion binding
B0046983molecular_functionprotein dimerization activity
C0003677molecular_functionDNA binding
C0003700molecular_functionDNA-binding transcription factor activity
C0005737cellular_componentcytoplasm
C0006355biological_processregulation of DNA-templated transcription
C0030026biological_processintracellular manganese ion homeostasis
C0030145molecular_functionmanganese ion binding
C0046872molecular_functionmetal ion binding
C0046914molecular_functiontransition metal ion binding
C0046983molecular_functionprotein dimerization activity
D0003677molecular_functionDNA binding
D0003700molecular_functionDNA-binding transcription factor activity
D0005737cellular_componentcytoplasm
D0006355biological_processregulation of DNA-templated transcription
D0030026biological_processintracellular manganese ion homeostasis
D0030145molecular_functionmanganese ion binding
D0046872molecular_functionmetal ion binding
D0046914molecular_functiontransition metal ion binding
D0046983molecular_functionprotein dimerization activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 150
ChainResidue
ASER106
ATRP107
AASN108
BLYS93

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 150
ChainResidue
ALYS93
BSER106
BTRP107
BASN108

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 B 151
ChainResidue
BVAL25
BSER26
BARG24

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 150
ChainResidue
BHIS35
BPRO36
BSER37
CSER106
CTRP107
CASN108
DLYS93

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 C 151
ChainResidue
CVAL25
CTYR54
CLYS56
CTYR57
CHOH157

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 D 150
ChainResidue
CHIS35
CPRO36
CSER37
CLYS93
DSER106
DTRP107
DASN108

site_idAC7
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 151
ChainResidue
DHIS35
DPRO36
DSER37

site_idAC8
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 A 151
ChainResidue
ATHR63
ASER64
DARG24
DVAL25
DSER26

site_idAC9
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 D 152
ChainResidue
DVAL34
DHIS35
DSER38

site_idBC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EPE D 300
ChainResidue
CVAL34
CHIS35
CSER38
CHOH159
DARG72
DTYR75
DTRP107

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:12847518, ECO:0000269|PubMed:16533030, ECO:0000269|PubMed:23298157
ChainResidueDetails
AASP8
BGLU99
BGLU102
BHIS103
CASP8
CGLU11
CHIS77
CGLU99
CGLU102
CHIS103
DASP8
AGLU11
DGLU11
DHIS77
DGLU99
DGLU102
DHIS103
AHIS77
AGLU99
AGLU102
AHIS103
BASP8
BGLU11
BHIS77

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PDB entries from 2024-09-11

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