4XGW

Crystal structure of Escherichia coli Flavin trafficking protein, an FMN transferase, E169K mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005515	molecular_function	protein binding
A	0005886	cellular_component	plasma membrane
A	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
A	0016740	molecular_function	transferase activity
A	0017013	biological_process	protein flavinylation
A	0046872	molecular_function	metal ion binding
A	1990204	cellular_component	oxidoreductase complex
B	0005515	molecular_function	protein binding
B	0005886	cellular_component	plasma membrane
B	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
B	0016740	molecular_function	transferase activity
B	0017013	biological_process	protein flavinylation
B	0046872	molecular_function	metal ion binding
B	1990204	cellular_component	oxidoreductase complex
C	0005515	molecular_function	protein binding
C	0005886	cellular_component	plasma membrane
C	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
C	0016740	molecular_function	transferase activity
C	0017013	biological_process	protein flavinylation
C	0046872	molecular_function	metal ion binding
C	1990204	cellular_component	oxidoreductase complex
D	0005515	molecular_function	protein binding
D	0005886	cellular_component	plasma membrane
D	0016651	molecular_function	oxidoreductase activity, acting on NAD(P)H
D	0016740	molecular_function	transferase activity
D	0017013	biological_process	protein flavinylation
D	0046872	molecular_function	metal ion binding
D	1990204	cellular_component	oxidoreductase complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue CA A 501

Chain	Residue
A	THR166
A	ASP280
A	ASP283
A	THR284
A	HOH743

---

site_id	AC2
Number of Residues	6
Details	binding site for residue NA A 502

Chain	Residue
A	HOH693
A	HOH698
A	LYS134
A	THR137
A	HOH618
A	HOH669

---

site_id	AC3
Number of Residues	5
Details	binding site for residue CA B 501

Chain	Residue
B	THR166
B	ASP280
B	ASP283
B	THR284
B	HOH669

---

site_id	AC4
Number of Residues	6
Details	binding site for residue CA C 501

Chain	Residue
C	THR166
C	ASP280
C	ASP283
C	THR284
C	HOH683
C	HOH730

---

site_id	AC5
Number of Residues	4
Details	binding site for residue NA C 502

Chain	Residue
C	LYS134
C	THR137
C	HOH651
C	HOH703

---

site_id	AC6
Number of Residues	5
Details	binding site for residue EDO C 503

Chain	Residue
C	LEU289
C	GLY290
C	PRO291
C	GLU292
C	LYS293

---

site_id	AC7
Number of Residues	1
Details	binding site for residue EDO C 504

Chain	Residue
C	GLN120

---

site_id	AC8
Number of Residues	5
Details	binding site for residue CA D 501

Chain	Residue
D	THR166
D	ASP280
D	ASP283
D	THR284
D	HOH759

---

site_id	AC9
Number of Residues	5
Details	binding site for residue NA D 502

Chain	Residue
D	LYS134
D	THR137
D	HOH699
D	HOH715
D	HOH754

---

site_id	AD1
Number of Residues	8
Details	binding site for residue EDO D 503

Chain	Residue
A	SER76
A	PRO77
D	PRO77
D	TRP78
D	PRO79
D	EDO504
D	HOH601
D	HOH723

---

site_id	AD2
Number of Residues	5
Details	binding site for residue EDO D 504

Chain	Residue
A	PRO77
A	TYR152
D	TRP78
D	EDO503
D	HOH679

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	28
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P41780","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	16
Details	Binding site: {"evidences":[{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"NOV-2006","submissionDatabase":"PDB data bank","title":"Crystal structure of a thiamine biosynthesis lipoprotein ApbE.","authoringGroup":["Northeast structural genomics consortium (NESG)"]}},{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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