Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1R2R

CRYSTAL STRUCTURE OF RABBIT MUSCLE TRIOSEPHOSPHATE ISOMERASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004807	molecular_function	triose-phosphate isomerase activity
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0008929	molecular_function	methylglyoxal synthase activity
A	0016829	molecular_function	lyase activity
A	0016853	molecular_function	isomerase activity
A	0019242	biological_process	methylglyoxal biosynthetic process
A	0019563	biological_process	glycerol catabolic process
A	0019682	biological_process	glyceraldehyde-3-phosphate metabolic process
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0042803	molecular_function	protein homodimerization activity
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
A	0061621	biological_process	canonical glycolysis
B	0004807	molecular_function	triose-phosphate isomerase activity
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006094	biological_process	gluconeogenesis
B	0006096	biological_process	glycolytic process
B	0008929	molecular_function	methylglyoxal synthase activity
B	0016829	molecular_function	lyase activity
B	0016853	molecular_function	isomerase activity
B	0019242	biological_process	methylglyoxal biosynthetic process
B	0019563	biological_process	glycerol catabolic process
B	0019682	biological_process	glyceraldehyde-3-phosphate metabolic process
B	0031625	molecular_function	ubiquitin protein ligase binding
B	0042803	molecular_function	protein homodimerization activity
B	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
B	0061621	biological_process	canonical glycolysis
C	0004807	molecular_function	triose-phosphate isomerase activity
C	0005737	cellular_component	cytoplasm
C	0005829	cellular_component	cytosol
C	0006094	biological_process	gluconeogenesis
C	0006096	biological_process	glycolytic process
C	0008929	molecular_function	methylglyoxal synthase activity
C	0016829	molecular_function	lyase activity
C	0016853	molecular_function	isomerase activity
C	0019242	biological_process	methylglyoxal biosynthetic process
C	0019563	biological_process	glycerol catabolic process
C	0019682	biological_process	glyceraldehyde-3-phosphate metabolic process
C	0031625	molecular_function	ubiquitin protein ligase binding
C	0042803	molecular_function	protein homodimerization activity
C	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
C	0061621	biological_process	canonical glycolysis
D	0004807	molecular_function	triose-phosphate isomerase activity
D	0005737	cellular_component	cytoplasm
D	0005829	cellular_component	cytosol
D	0006094	biological_process	gluconeogenesis
D	0006096	biological_process	glycolytic process
D	0008929	molecular_function	methylglyoxal synthase activity
D	0016829	molecular_function	lyase activity
D	0016853	molecular_function	isomerase activity
D	0019242	biological_process	methylglyoxal biosynthetic process
D	0019563	biological_process	glycerol catabolic process
D	0019682	biological_process	glyceraldehyde-3-phosphate metabolic process
D	0031625	molecular_function	ubiquitin protein ligase binding
D	0042803	molecular_function	protein homodimerization activity
D	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
D	0061621	biological_process	canonical glycolysis

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS A 249

Chain	Residue
A	THR89
A	TRP90
A	GLY122

site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMS A 253

Chain	Residue
A	LYS218
A	SER222
A	ALA246
A	LYS247

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS A 255

Chain	Residue
A	HOH545
D	GLU135
D	ALA136
A	LYS68
A	HOH311

site_id	AC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG B 257

Chain	Residue
B	ARG99
B	ASP106
B	GLN146
B	HOH538
B	HOH822

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS B 249

Chain	Residue
B	THR89
B	TRP90
B	GLY120
B	GLY122
B	LYS159

site_id	AC6
Number of Residues	1
Details	BINDING SITE FOR RESIDUE DMS B 250

Chain	Residue
B	ASN20

site_id	AC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS B 252

Chain	Residue
B	ARG134
B	GLU183
B	LYS187

site_id	AC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMS B 255

Chain	Residue
A	GLY103
A	LEU108
A	HOH515
A	HOH543
B	VAL101
D	LYS141

site_id	AC9
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS B 256

Chain	Residue
B	SER197
B	ASP198
B	HOH613

site_id	BC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG B 261

Chain	Residue
B	HOH838
B	HOH840
B	HOH1156
C	HOH832
C	HOH834
C	HOH836

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG C 260

Chain	Residue
C	HOH540
C	HOH542
C	HOH824
C	HOH826
C	HOH828
C	HOH830

site_id	BC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE MG B 263

Chain	Residue
C	HOH846
C	HOH848

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG C 262

Chain	Residue
C	SER96
C	HOH842
C	HOH844

site_id	BC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMS C 249

Chain	Residue
C	THR89
C	TRP90

site_id	BC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE DMS C 250

Chain	Residue
C	ASN20
C	HOH1051

site_id	BC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE DMS C 251

Chain	Residue
C	GLY16
C	ARG17
C	ASN20
C	HOH971
C	HOH1051
C	HOH1097
D	ASN71
D	TRS258

site_id	BC8
Number of Residues	4
Details	BINDING SITE FOR RESIDUE DMS C 254

Chain	Residue
A	SER194
A	HOH492
B	GLU186
C	ASP132

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE DMS C 257

Chain	Residue
C	LYS130
C	LEU131
C	VAL167
C	HOH880
C	HOH889

site_id	CC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE DMS D 254

Chain	Residue
B	ALA136
C	HOH975
C	HOH1104
C	HOH1114
D	VAL101
D	PHE102

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE TRS D 258

Chain	Residue
C	TRP191
C	ASN195
C	DMS251
C	HOH881
C	HOH1035
D	ASN71
D	HOH1267

site_id	CC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE TRS C 259

Chain	Residue
C	VAL149
C	ASP152
C	ASN153
C	LYS237
C	HOH960

site_id	CC4
Number of Residues	7
Details	BINDING SITE FOR RESIDUE MG D 249

Chain	Residue
B	HOH835
B	HOH1160
B	HOH1166
D	HOH850
D	HOH1158
D	HOH1162
D	HOH1164

site_id	CC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 255

Chain	Residue
D	TRP191
D	HOH852
D	HOH854
D	HOH1172
D	PHE144

site_id	CC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 256

Chain	Residue
D	ASP156
D	THR177
D	HOH544
D	HOH546
D	HOH1386

site_id	CC7
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG D 257

Chain	Residue
D	SER96
D	HOH856
D	HOH1168

site_id	CC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS D 250

Chain	Residue
D	ASN20
D	LEU21
D	LEU236

site_id	CC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE DMS D 252

Chain	Residue
D	ARG134
D	THR139
D	GLU183
D	VAL184
D	LYS187
D	HOH1195
D	HOH1349

site_id	DC1
Number of Residues	3
Details	BINDING SITE FOR RESIDUE DMS D 253

Chain	Residue
C	SER222
C	PRO224
D	SER222

Functional Information from PROSITE/UniProt

site_id	PS00171
Number of Residues	11
Details	TIM_1 Triosephosphate isomerase active site. AYEPVWAIGTG

Chain	Residue	Details
A	ALA163-GLY173

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	Active site: {"description":"Electrophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10127","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	4
Details	Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"4922541","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	8
Details	Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU10127","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P60174","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	8
Details	Modified residue: {"description":"Deamidated asparagine","evidences":[{"source":"PubMed","id":"7574709","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	8
Details	Modified residue: {"description":"3'-nitrotyrosine","evidences":[{"source":"UniProtKB","id":"P17751","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	12
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P60174","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	8
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P48500","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	4
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P17751","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	8
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P17751","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	4
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P17751","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P17751","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	4
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P60174","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)","evidences":[{"source":"UniProtKB","id":"P60174","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	5
Details	Annotated By Reference To The Literature 1hti

Chain	Residue	Details
A	LYS13
A	HIS95
A	ASN11
A	GLU165
A	GLY171

site_id	CSA2
Number of Residues	5
Details	Annotated By Reference To The Literature 1hti

Chain	Residue	Details
B	LYS13
B	HIS95
B	ASN11
B	GLU165
B	GLY171

site_id	CSA3
Number of Residues	5
Details	Annotated By Reference To The Literature 1hti

Chain	Residue	Details
C	LYS13
C	HIS95
C	ASN11
C	GLU165
C	GLY171

site_id	CSA4
Number of Residues	5
Details	Annotated By Reference To The Literature 1hti

Chain	Residue	Details
D	LYS13
D	HIS95
D	ASN11
D	GLU165
D	GLY171

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