Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7SX1

human triosephosphate isomerase mutant v154m

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004807	molecular_function	triose-phosphate isomerase activity
A	0005515	molecular_function	protein binding
A	0005615	cellular_component	extracellular space
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006006	biological_process	glucose metabolic process
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
A	0070062	cellular_component	extracellular exosome
B	0004807	molecular_function	triose-phosphate isomerase activity
B	0005515	molecular_function	protein binding
B	0005615	cellular_component	extracellular space
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0006006	biological_process	glucose metabolic process
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
B	0070062	cellular_component	extracellular exosome

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	2
Details	ACT_SITE: Electrophile => ECO:0000255\|PROSITE-ProRule:PRU10127, ECO:0000269\|PubMed:8061610

Chain	Residue	Details
A	HIS95
B	HIS95

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000255\|PROSITE-ProRule:PRU10127, ECO:0000269\|PubMed:8061610

Chain	Residue	Details
A	GLU165
B	GLU165

site_id	SWS_FT_FI3
Number of Residues	4
Details	BINDING: BINDING => ECO:0000255\|PROSITE-ProRule:PRU10127, ECO:0000269\|PubMed:8061610

Chain	Residue	Details
A	ASN11
A	LYS13
B	ASN11
B	LYS13

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
A	LYS13
A	LYS237
B	LYS13
B	LYS237

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:16807684, ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:17693683, ECO:0007744\|PubMed:17924679, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19367720, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER20
B	SER20

site_id	SWS_FT_FI6
Number of Residues	4
Details	MOD_RES: 3'-nitrotyrosine => ECO:0000250\|UniProtKB:P17751

Chain	Residue	Details
A	TYR67
A	TYR208
B	TYR67
B	TYR208

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
A	SER79
B	SER79

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P48500

Chain	Residue	Details
A	SER105
A	SER197
B	SER105
B	SER197

site_id	SWS_FT_FI9
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P17751

Chain	Residue	Details
A	LYS148
B	LYS148

site_id	SWS_FT_FI10
Number of Residues	4
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P17751

Chain	Residue	Details
A	LYS155
A	LYS193
B	LYS155
B	LYS193

site_id	SWS_FT_FI11
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P17751

Chain	Residue	Details
A	SER158
B	SER158

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P17751

Chain	Residue	Details
A	THR172
B	THR172

site_id	SWS_FT_FI13
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER211
B	SER211

site_id	SWS_FT_FI14
Number of Residues	2
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	THR213
B	THR213

site_id	SWS_FT_FI15
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
A	SER222
B	SER222

site_id	SWS_FT_FI16
Number of Residues	4
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1) => ECO:0007744\|PubMed:25114211

Chain	Residue	Details
A	LYS141
B	LYS141

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