2P4T

Structure of the Q67H mutant of R67 dihydrofolate reductase-NADP+ complex reveals a novel cofactor binding mode

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004146	molecular_function	dihydrofolate reductase activity
A	0009410	biological_process	response to xenobiotic stimulus

Functional Information from PDB Data

site_id	AC1
Number of Residues	18
Details	BINDING SITE FOR RESIDUE NAP A 157

Chain	Residue
A	LYS32
A	HOH145
A	HOH146
A	HOH146
A	HOH146
A	HOH147
A	HOH149
A	HOH149
A	HOH151
A	HOH152
A	ALA36
A	VAL66
A	HIS67
A	ILE68
A	ILE68
A	TYR69
A	HOH144
A	HOH145

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	BINDING: BINDING => ECO:0000269|PubMed:17473013, ECO:0000269|PubMed:18052202, ECO:0007744|PDB:2P4T, ECO:0007744|PDB:2RK1, ECO:0007744|PDB:2RK2

Chain	Residue	Details
A	LYS32
A	VAL66

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site_id	SWS_FT_FI2
Number of Residues	1
Details	BINDING: BINDING => ECO:0000269|PubMed:18052202, ECO:0007744|PDB:2RK1

Chain	Residue	Details
A	ILE68

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	4
Details	Annotated By Reference To The Literature 1vie

Chain	Residue	Details
A	ILE68
A	LYS32
A	TYR69
A	HIS67

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site_id	MCSA1
Number of Residues	4
Details	M-CSA 752

Chain	Residue	Details
A	LYS32	electrostatic stabiliser
A	HIS67	electrostatic stabiliser
A	ILE68	electrostatic stabiliser
A	TYR69	electrostatic stabiliser

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