Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1WUQ

Structure of GTP cyclohydrolase I Complexed with 8-oxo-GTP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0003934	molecular_function	GTP cyclohydrolase I activity
A	0005525	molecular_function	GTP binding
A	0005737	cellular_component	cytoplasm
A	0006729	biological_process	tetrahydrobiopterin biosynthetic process
A	0006730	biological_process	one-carbon metabolic process
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0046654	biological_process	tetrahydrofolate biosynthetic process
A	0046872	molecular_function	metal ion binding
B	0000166	molecular_function	nucleotide binding
B	0003934	molecular_function	GTP cyclohydrolase I activity
B	0005525	molecular_function	GTP binding
B	0005737	cellular_component	cytoplasm
B	0006729	biological_process	tetrahydrobiopterin biosynthetic process
B	0006730	biological_process	one-carbon metabolic process
B	0008270	molecular_function	zinc ion binding
B	0016787	molecular_function	hydrolase activity
B	0046654	biological_process	tetrahydrofolate biosynthetic process
B	0046872	molecular_function	metal ion binding
C	0000166	molecular_function	nucleotide binding
C	0003934	molecular_function	GTP cyclohydrolase I activity
C	0005525	molecular_function	GTP binding
C	0005737	cellular_component	cytoplasm
C	0006729	biological_process	tetrahydrobiopterin biosynthetic process
C	0006730	biological_process	one-carbon metabolic process
C	0008270	molecular_function	zinc ion binding
C	0016787	molecular_function	hydrolase activity
C	0046654	biological_process	tetrahydrofolate biosynthetic process
C	0046872	molecular_function	metal ion binding
D	0000166	molecular_function	nucleotide binding
D	0003934	molecular_function	GTP cyclohydrolase I activity
D	0005525	molecular_function	GTP binding
D	0005737	cellular_component	cytoplasm
D	0006729	biological_process	tetrahydrobiopterin biosynthetic process
D	0006730	biological_process	one-carbon metabolic process
D	0008270	molecular_function	zinc ion binding
D	0016787	molecular_function	hydrolase activity
D	0046654	biological_process	tetrahydrofolate biosynthetic process
D	0046872	molecular_function	metal ion binding
E	0000166	molecular_function	nucleotide binding
E	0003934	molecular_function	GTP cyclohydrolase I activity
E	0005525	molecular_function	GTP binding
E	0005737	cellular_component	cytoplasm
E	0006729	biological_process	tetrahydrobiopterin biosynthetic process
E	0006730	biological_process	one-carbon metabolic process
E	0008270	molecular_function	zinc ion binding
E	0016787	molecular_function	hydrolase activity
E	0046654	biological_process	tetrahydrofolate biosynthetic process
E	0046872	molecular_function	metal ion binding

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN A 1001

Chain	Residue
A	CYS108
A	HIS111
A	CYS179
A	8GT811

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN B 1002

Chain	Residue
B	CYS108
B	HIS111
B	CYS179
C	8GT812

site_id	AC3
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN C 1003

Chain	Residue
C	HIS111
C	CYS179
C	8GT813
C	CYS108

site_id	AC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN D 1004

Chain	Residue
D	CYS108
D	HIS111
D	CYS179
D	8GT814

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE ZN E 1005

Chain	Residue
A	8GT815
E	CYS108
E	HIS111
E	CYS179

site_id	AC6
Number of Residues	24
Details	BINDING SITE FOR RESIDUE 8GT A 811

Chain	Residue
A	CYS108
A	HIS110
A	HIS111
A	VAL148
A	GLN149
A	GLU150
A	HIS177
A	CYS179
A	ARG183
A	ZN1001
A	HOH1003
A	HOH1006
A	HOH1011
A	HOH1049
B	ALA87
B	PHE89
B	LEU130
B	GLY131
B	LEU132
B	SER133
B	LYS134
B	ARG137
E	ARG64
E	HOH1031

site_id	AC7
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 8GT C 812

Chain	Residue
B	CYS108
B	HIS110
B	HIS111
B	VAL148
B	GLN149
B	GLU150
B	HIS177
B	CYS179
B	ARG183
B	ZN1002
B	HOH1031
C	ALA87
C	LEU130
C	GLY131
C	LEU132
C	SER133
C	LYS134
C	ARG137
C	HOH1009
D	ARG64
D	HOH1044

site_id	AC8
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 8GT C 813

Chain	Residue
C	ARG64
C	CYS108
C	HIS110
C	HIS111
C	VAL148
C	GLN149
C	GLU150
C	HIS177
C	CYS179
C	ARG183
C	ZN1003
C	HOH1008
C	HOH1027
D	ALA87
D	LEU130
D	GLY131
D	LEU132
D	SER133
D	LYS134
D	ARG137

site_id	AC9
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 8GT D 814

Chain	Residue
E	ALA87
E	LEU130
E	GLY131
E	LEU132
E	SER133
E	LYS134
E	ARG137
B	ARG64
D	CYS108
D	HIS110
D	HIS111
D	VAL148
D	GLN149
D	GLU150
D	CYS179
D	ARG183
D	ZN1004
D	HOH1006
D	HOH1008
D	HOH1009
D	HOH1034

site_id	BC1
Number of Residues	21
Details	BINDING SITE FOR RESIDUE 8GT A 815

Chain	Residue
A	ARG64
A	LEU130
A	GLY131
A	LEU132
A	SER133
A	LYS134
A	ARG137
A	HOH1016
A	HOH1043
A	HOH1061
E	CYS108
E	HIS110
E	HIS111
E	VAL148
E	GLN149
E	GLU150
E	CYS179
E	ARG183
E	ZN1005
E	HOH1013
E	HOH1021

Functional Information from PROSITE/UniProt

site_id	PS00859
Number of Residues	17
Details	GTP_CYCLOHYDROL_1_1 GTP cyclohydrolase I signature 1. EMVvvKGVefySmCEHH

Chain	Residue	Details
A	GLU95-HIS111

Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1gtp

Chain	Residue	Details
A	HIS177
A	HIS110

site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1gtp

Chain	Residue	Details
B	HIS177
B	HIS110

site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1gtp

Chain	Residue	Details
C	HIS177
C	HIS110

site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1gtp

Chain	Residue	Details
D	HIS177
D	HIS110

site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1gtp

Chain	Residue	Details
E	HIS177
E	HIS110

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)
		EDMap 2fo-fc (MTZ)