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4Z7F

Crystal structure of FolT bound with folic acid

Functional Information from GO Data
ChainGOidnamespacecontents
A0016020cellular_componentmembrane
A0022857molecular_functiontransmembrane transporter activity
A0055085biological_processtransmembrane transport
B0016020cellular_componentmembrane
B0022857molecular_functiontransmembrane transporter activity
B0055085biological_processtransmembrane transport
C0016020cellular_componentmembrane
C0022857molecular_functiontransmembrane transporter activity
C0055085biological_processtransmembrane transport
D0016020cellular_componentmembrane
D0022857molecular_functiontransmembrane transporter activity
D0055085biological_processtransmembrane transport
E0016020cellular_componentmembrane
E0022857molecular_functiontransmembrane transporter activity
E0055085biological_processtransmembrane transport
F0016020cellular_componentmembrane
F0022857molecular_functiontransmembrane transporter activity
F0055085biological_processtransmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues16
Detailsbinding site for residue FOL A 201
ChainResidue
ATHR32
APHE77
APHE80
ATHR81
AASN117
ATHR121
AARG142
ALYS145
ALEU35
ALYS36
ASER38
AASP64
AMET68
AALA74
AGLY75
ATYR76

site_idAC2
Number of Residues14
Detailsbinding site for residue FOL B 201
ChainResidue
BLEU35
BLYS36
BASP64
BMET68
BALA74
BGLY75
BTYR76
BPHE77
BPHE80
BTHR81
BASN117
BTHR121
BARG142
BLYS145

site_idAC3
Number of Residues14
Detailsbinding site for residue FOL C 201
ChainResidue
CARG26
CLYS36
CASP64
CALA74
CGLY75
CTYR76
CPHE77
CPHE80
CTHR81
CASN117
CTHR121
CLEU125
CARG142
CLYS145

site_idAC4
Number of Residues11
Detailsbinding site for residue FOL D 201
ChainResidue
DARG26
DTHR33
DLEU35
DLYS36
DSER38
DASP64
DMET68
DPHE80
DASN117
DTHR121
DLYS145

site_idAC5
Number of Residues11
Detailsbinding site for residue FOL E 201
ChainResidue
ETHR32
ELEU35
ELYS36
EMET68
EALA74
EGLY75
ETYR76
EPHE77
EPHE80
EASN117
ETHR121

site_idAC6
Number of Residues11
Detailsbinding site for residue FOL F 201
ChainResidue
FPHE34
FLEU35
FLYS36
FSER38
FMET68
FLYS73
FALA74
FPHE80
FASN117
FTHR121
FARG142

site_idAC7
Number of Residues7
Detailsbinding site for Ligand PRO E 43 bound to THR E 40
ChainResidue
ETHR40
EPHE41
EILE42
EGLU44
ESER45
ELEU46
EILE47

site_idAC8
Number of Residues11
Detailsbinding site for Di-peptide MET B 14 and PHE B 51
ChainResidue
BSER10
BILE11
BALA12
BLEU13
BGLY15
BVAL16
BLEU17
BILE18
BILE47
BILE50
BGLY52

site_idAC9
Number of Residues6
Detailsbinding site for Di-peptide TYR B 30 and LYS B 36
ChainResidue
BLYS145
BFOL201
BALA29
BGLU31
BLEU35
BILE37

site_idAD1
Number of Residues6
Detailsbinding site for Di-peptide TYR B 30 and LYS B 36
ChainResidue
BALA29
BGLU31
BLEU35
BILE37
BLYS145
BFOL201

site_idAD2
Number of Residues12
Detailsbinding site for Di-peptide MET B 49 and MET B 100
ChainResidue
BSER45
BLEU46
BILE47
BGLY48
BILE50
BTYR95
BTYR96
BLYS98
BGLU99
BTHR101
BLEU160
BGLY161

site_idAD3
Number of Residues16
Detailsbinding site for Di-peptide LEU E 17 and ILE E 47
ChainResidue
ELEU13
EMET14
EGLY15
EVAL16
EILE18
EALA19
EVAL20
EVAL21
EPRO43
EGLU44
ESER45
ELEU46
EGLY48
EMET49
EILE50
EPHE51

site_idAD4
Number of Residues12
Detailsbinding site for Di-peptide ILE E 42 and LEU E 160
ChainResidue
ETHR40
EPHE41
EPRO43
EGLU44
ESER45
ELEU46
EMET49
EALA156
ETHR157
ETYR158
ETYR159
EGLY161

site_idAD5
Number of Residues10
Detailsbinding site for Di-peptide GLY E 79 and TRP E 124
ChainResidue
EPHE77
EPRO78
EPHE80
ETHR81
ELEU82
EASN83
ELEU120
EPRO122
ELEU123
ELEU125

site_idAD6
Number of Residues10
Detailsbinding site for Di-peptide GLY E 79 and TRP E 124
ChainResidue
EPHE77
EPRO78
EPHE80
ETHR81
ELEU82
EASN83
ELEU120
EPRO122
ELEU123
ELEU125

site_idAD7
Number of Residues10
Detailsbinding site for Di-peptide GLY E 79 and TRP E 124
ChainResidue
EPHE77
EPRO78
EPHE80
ETHR81
ELEU82
EASN83
ELEU120
EPRO122
ELEU123
ELEU125

site_idAD8
Number of Residues13
Detailsbinding site for Di-peptide MET F 14 and PHE F 51
ChainResidue
FSER10
FALA12
FLEU13
FGLY15
FVAL16
FLEU17
FILE18
FILE47
FGLY48
FILE50
FGLY52
FTRP55
FALA56

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PDB entries from 2024-04-24

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