Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

2Y85

CRYSTAL STRUCTURE OF MYCOBACTERIUM TUBERCULOSIS PHOSPHORIBOSYL ISOMERASE WITH BOUND RCDRP

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000105	biological_process	L-histidine biosynthetic process
A	0000162	biological_process	tryptophan biosynthetic process
A	0003949	molecular_function	1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity
A	0004640	molecular_function	phosphoribosylanthranilate isomerase activity
A	0005737	cellular_component	cytoplasm
A	0016853	molecular_function	isomerase activity
B	0000105	biological_process	L-histidine biosynthetic process
B	0000162	biological_process	tryptophan biosynthetic process
B	0003949	molecular_function	1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity
B	0004640	molecular_function	phosphoribosylanthranilate isomerase activity
B	0005737	cellular_component	cytoplasm
B	0016853	molecular_function	isomerase activity
C	0000105	biological_process	L-histidine biosynthetic process
C	0000162	biological_process	tryptophan biosynthetic process
C	0003949	molecular_function	1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity
C	0004640	molecular_function	phosphoribosylanthranilate isomerase activity
C	0005737	cellular_component	cytoplasm
C	0016853	molecular_function	isomerase activity
D	0000105	biological_process	L-histidine biosynthetic process
D	0000162	biological_process	tryptophan biosynthetic process
D	0003949	molecular_function	1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity
D	0004640	molecular_function	phosphoribosylanthranilate isomerase activity
D	0005737	cellular_component	cytoplasm
D	0016853	molecular_function	isomerase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 1245

Chain	Residue
A	GLY201
A	GLY202
A	VAL203
A	ILE224
A	1371247

site_id	AC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CL A 1246

Chain	Residue
A	GLY104
A	GLY82
A	GLY83
A	ILE84
A	ASN102

site_id	AC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 137 A 1247

Chain	Residue
A	ALA9
A	ASP11
A	HIS50
A	VAL52
A	LEU54
A	ALA57
A	SER81
A	ARG143
A	ASP175
A	GLY176
A	SER200
A	GLY201
A	GLY202
A	GLY226
A	LYS227
A	NA1245
A	HOH2033
A	HOH2034
A	HOH2035
A	HOH2036

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 1248

Chain	Residue
A	LEU129
A	ASP130
A	ARG143
A	VAL168
A	THR170

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA A 1249

Chain	Residue
A	ILE172
A	THR173
A	ASP175
A	THR177
B	GLN132

site_id	AC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 1245

Chain	Residue
B	GLY201
B	GLY202
B	VAL203
B	ILE224
B	1371247

site_id	AC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE CL B 1246

Chain	Residue
B	SER81
B	GLY82
B	GLY83
B	ILE84
B	ASN102
B	GLY104
B	HOH2047

site_id	AC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE 137 B 1247

Chain	Residue
B	ALA9
B	ASP11
B	HIS50
B	VAL52
B	SER81
B	GLY82
B	ARG143
B	ASP175
B	GLY176
B	SER200
B	GLY201
B	GLY202
B	VAL225
B	GLY226
B	LYS227
B	NA1245
B	HOH2047
B	HOH2048
B	HOH2049

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA B 1248

Chain	Residue
B	LEU129
B	ASP130
B	VAL168
B	VAL169
B	THR170

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA C 1245

Chain	Residue
C	GLY201
C	GLY202
C	VAL203
C	ILE224
C	1371247

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CL C 1246

Chain	Residue
C	SER81
C	GLY82
C	GLY83
C	ILE84
C	ASN102
C	GLY104

site_id	BC3
Number of Residues	20
Details	BINDING SITE FOR RESIDUE 137 C 1247

Chain	Residue
C	GLY201
C	GLY202
C	GLY226
C	LYS227
C	NA1245
C	HOH2049
C	HOH2050
C	HOH2051
C	ALA9
C	ASP11
C	HIS50
C	VAL52
C	LEU54
C	ALA57
C	SER81
C	GLY82
C	ARG143
C	ASP175
C	GLY176
C	SER200

site_id	BC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 1248

Chain	Residue
C	LEU129
C	ASP130
C	VAL168
C	THR170

site_id	BC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 1249

Chain	Residue
C	ILE172
C	THR173
C	LYS174
C	ASP175

site_id	BC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 1245

Chain	Residue
D	GLY201
D	GLY202
D	VAL203
D	ILE224
D	1371247

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE CL D 1246

Chain	Residue
D	SER81
D	GLY82
D	GLY83
D	ILE84
D	ASN102
D	GLY104
D	HOH2015
D	HOH2050

site_id	BC8
Number of Residues	19
Details	BINDING SITE FOR RESIDUE 137 D 1247

Chain	Residue
D	ALA9
D	ASP11
D	HIS50
D	VAL52
D	SER81
D	GLY82
D	ARG143
D	ASP175
D	GLY176
D	SER200
D	GLY201
D	GLY202
D	GLY226
D	LYS227
D	NA1245
D	HOH2040
D	HOH2050
D	HOH2051
D	HOH2052

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA D 1248

Chain	Residue
D	LEU129
D	ASP130
D	ARG143
D	VAL168
D	THR170

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D 1249

Chain	Residue
D	ILE172
D	THR173
D	LYS174
D	ASP175

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Proton acceptor => ECO:0000250

Chain	Residue	Details
A	ASP11
B	ASP11
C	ASP11
D	ASP11

site_id	SWS_FT_FI2
Number of Residues	4
Details	ACT_SITE: Proton donor => ECO:0000250

Chain	Residue	Details
A	ASP130
B	ASP130
C	ASP130
D	ASP130

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