2CFI

The hydrolase domain of human 10-FTHFD in complex with 6- formyltetrahydropterin

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0003824	molecular_function	catalytic activity
A	0009058	biological_process	biosynthetic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A1308

Chain	Residue
A	ARG112
A	LYS128
A	LYS129

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A1309

Chain	Residue
A	ARG60
A	PHE89
A	PRO264
A	GLY265

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site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE SO4 A1310

Chain	Residue
A	HOH2300
A	HOH2301
A	HOH2302
A	ARG112
A	GLY197

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site_id	AC4
Number of Residues	12
Details	BINDING SITE FOR RESIDUE ZZZ A1311

Chain	Residue
A	CYS86
A	SER87
A	GLN88
A	PHE89
A	ILE90
A	ILE95
A	ILE104
A	PHE135
A	ASP138
A	GLY140
A	ASP142
A	HOH2136

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Functional Information from PROSITE/UniProt

site_id	PS00373
Number of Residues	24
Details	GART Phosphoribosylglycinamide formyltransferase active site. GfSIfWAdDgLDtGdlLlqkeceV

Chain	Residue	Details
A	GLY131-VAL154

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000250|UniProtKB:P28037

Chain	Residue	Details
A	HIS106

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site_id	SWS_FT_FI2
Number of Residues	2
Details	BINDING: BINDING => ECO:0000305|PubMed:17057331, ECO:0007744|PDB:2CFI

Chain	Residue	Details
A	GLN88
A	ASP142

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site_id	SWS_FT_FI3
Number of Residues	1
Details	SITE: Essential for catalytic activity => ECO:0000250|UniProtKB:P28037

Chain	Residue	Details
A	ASP142

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site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER9

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site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q8R0Y6

Chain	Residue	Details
A	LYS38

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