5O22

E. coli FolD in complex with carolacton

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0004477	molecular_function	methenyltetrahydrofolate cyclohydrolase activity
A	0004488	molecular_function	methylenetetrahydrofolate dehydrogenase (NADP+) activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0016491	molecular_function	oxidoreductase activity
A	0035999	biological_process	tetrahydrofolate interconversion
A	0042803	molecular_function	protein homodimerization activity
B	0003824	molecular_function	catalytic activity
B	0004477	molecular_function	methenyltetrahydrofolate cyclohydrolase activity
B	0004488	molecular_function	methylenetetrahydrofolate dehydrogenase (NADP+) activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0016491	molecular_function	oxidoreductase activity
B	0035999	biological_process	tetrahydrofolate interconversion
B	0042803	molecular_function	protein homodimerization activity
C	0003824	molecular_function	catalytic activity
C	0004477	molecular_function	methenyltetrahydrofolate cyclohydrolase activity
C	0004488	molecular_function	methylenetetrahydrofolate dehydrogenase (NADP+) activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0016491	molecular_function	oxidoreductase activity
C	0035999	biological_process	tetrahydrofolate interconversion
C	0042803	molecular_function	protein homodimerization activity
D	0003824	molecular_function	catalytic activity
D	0004477	molecular_function	methenyltetrahydrofolate cyclohydrolase activity
D	0004488	molecular_function	methylenetetrahydrofolate dehydrogenase (NADP+) activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0016491	molecular_function	oxidoreductase activity
D	0035999	biological_process	tetrahydrofolate interconversion
D	0042803	molecular_function	protein homodimerization activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	12
Details	binding site for residue C3R A 301

Chain	Residue
A	LYS54
A	HOH447
A	HOH467
A	HOH469
A	ILE170
A	PRO260
A	GLY261
A	GLY264
A	PRO265
A	HOH423
A	HOH425
A	HOH431

---

site_id	AC2
Number of Residues	10
Details	binding site for residue C3R B 301

Chain	Residue
B	LYS54
B	ILE170
B	PRO260
B	GLY261
B	GLY264
B	PRO265
B	VAL268
B	HOH418
B	HOH429
B	HOH482

---

site_id	AC3
Number of Residues	10
Details	binding site for residue C3R C 301

Chain	Residue
C	TYR50
C	LYS54
C	PRO260
C	GLY261
C	GLY264
C	PRO265
C	THR267
C	HOH407
C	HOH473
C	HOH480

---

site_id	AC4
Number of Residues	10
Details	binding site for residue C3R D 301

Chain	Residue
D	TYR50
D	LYS54
D	PRO260
D	GLY261
D	GLY264
D	PRO265
D	VAL268
D	HOH413
D	HOH414
D	HOH441

---

Functional Information from PROSITE/UniProt

site_id	PS00766
Number of Residues	26
Details	THF_DHG_CYH_1 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 1. EaELLelIdtLNaDntidgILVQLPL

Chain	Residue	Details
C	GLU76-LEU101
D	GLU76-LEU101
A	GLU76-LEU101
B	GLU76-LEU101

---

site_id	PS00767
Number of Residues	9
Details	THF_DHG_CYH_2 Tetrahydrofolate dehydrogenase/cyclohydrolase signature 2. PGGVGPMTV

Chain	Residue	Details
C	PRO260-VAL268
D	PRO260-VAL268
A	PRO260-VAL268
B	PRO260-VAL268

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01576","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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