Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

6M61

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) with inhibitor heptelidic acid

Functional Information from GO Data

Chain	GOid	namespace	contents
O	0000226	biological_process	microtubule cytoskeleton organization
O	0001819	biological_process	positive regulation of cytokine production
O	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
O	0005515	molecular_function	protein binding
O	0005634	cellular_component	nucleus
O	0005737	cellular_component	cytoplasm
O	0005811	cellular_component	lipid droplet
O	0005829	cellular_component	cytosol
O	0005856	cellular_component	cytoskeleton
O	0005886	cellular_component	plasma membrane
O	0006006	biological_process	glucose metabolic process
O	0006096	biological_process	glycolytic process
O	0006417	biological_process	regulation of translation
O	0006915	biological_process	apoptotic process
O	0008017	molecular_function	microtubule binding
O	0010951	biological_process	negative regulation of endopeptidase activity
O	0015630	cellular_component	microtubule cytoskeleton
O	0016020	cellular_component	membrane
O	0016241	biological_process	regulation of macroautophagy
O	0016491	molecular_function	oxidoreductase activity
O	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
O	0016740	molecular_function	transferase activity
O	0017148	biological_process	negative regulation of translation
O	0019828	molecular_function	aspartic-type endopeptidase inhibitor activity
O	0031640	biological_process	killing of cells of another organism
O	0031965	cellular_component	nuclear membrane
O	0031982	cellular_component	vesicle
O	0032481	biological_process	positive regulation of type I interferon production
O	0035605	molecular_function	peptidyl-cysteine S-nitrosylase activity
O	0035606	biological_process	peptidyl-cysteine S-trans-nitrosylation
O	0042802	molecular_function	identical protein binding
O	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
O	0043231	cellular_component	intracellular membrane-bounded organelle
O	0045087	biological_process	innate immune response
O	0048471	cellular_component	perinuclear region of cytoplasm
O	0050661	molecular_function	NADP binding
O	0050821	biological_process	protein stabilization
O	0050832	biological_process	defense response to fungus
O	0051287	molecular_function	NAD binding
O	0051402	biological_process	neuron apoptotic process
O	0051873	biological_process	killing by host of symbiont cells
O	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
O	0070062	cellular_component	extracellular exosome
O	0071346	biological_process	cellular response to type II interferon
O	0097452	cellular_component	GAIT complex
O	0097718	molecular_function	disordered domain specific binding
O	1990904	cellular_component	ribonucleoprotein complex
P	0000226	biological_process	microtubule cytoskeleton organization
P	0001819	biological_process	positive regulation of cytokine production
P	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
P	0005515	molecular_function	protein binding
P	0005634	cellular_component	nucleus
P	0005737	cellular_component	cytoplasm
P	0005811	cellular_component	lipid droplet
P	0005829	cellular_component	cytosol
P	0005856	cellular_component	cytoskeleton
P	0005886	cellular_component	plasma membrane
P	0006006	biological_process	glucose metabolic process
P	0006096	biological_process	glycolytic process
P	0006417	biological_process	regulation of translation
P	0006915	biological_process	apoptotic process
P	0008017	molecular_function	microtubule binding
P	0010951	biological_process	negative regulation of endopeptidase activity
P	0015630	cellular_component	microtubule cytoskeleton
P	0016020	cellular_component	membrane
P	0016241	biological_process	regulation of macroautophagy
P	0016491	molecular_function	oxidoreductase activity
P	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
P	0016740	molecular_function	transferase activity
P	0017148	biological_process	negative regulation of translation
P	0019828	molecular_function	aspartic-type endopeptidase inhibitor activity
P	0031640	biological_process	killing of cells of another organism
P	0031965	cellular_component	nuclear membrane
P	0031982	cellular_component	vesicle
P	0032481	biological_process	positive regulation of type I interferon production
P	0035605	molecular_function	peptidyl-cysteine S-nitrosylase activity
P	0035606	biological_process	peptidyl-cysteine S-trans-nitrosylation
P	0042802	molecular_function	identical protein binding
P	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
P	0043231	cellular_component	intracellular membrane-bounded organelle
P	0045087	biological_process	innate immune response
P	0048471	cellular_component	perinuclear region of cytoplasm
P	0050661	molecular_function	NADP binding
P	0050821	biological_process	protein stabilization
P	0050832	biological_process	defense response to fungus
P	0051287	molecular_function	NAD binding
P	0051402	biological_process	neuron apoptotic process
P	0051873	biological_process	killing by host of symbiont cells
P	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
P	0070062	cellular_component	extracellular exosome
P	0071346	biological_process	cellular response to type II interferon
P	0097452	cellular_component	GAIT complex
P	0097718	molecular_function	disordered domain specific binding
P	1990904	cellular_component	ribonucleoprotein complex
Q	0000226	biological_process	microtubule cytoskeleton organization
Q	0001819	biological_process	positive regulation of cytokine production
Q	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
Q	0005515	molecular_function	protein binding
Q	0005634	cellular_component	nucleus
Q	0005737	cellular_component	cytoplasm
Q	0005811	cellular_component	lipid droplet
Q	0005829	cellular_component	cytosol
Q	0005856	cellular_component	cytoskeleton
Q	0005886	cellular_component	plasma membrane
Q	0006006	biological_process	glucose metabolic process
Q	0006096	biological_process	glycolytic process
Q	0006417	biological_process	regulation of translation
Q	0006915	biological_process	apoptotic process
Q	0008017	molecular_function	microtubule binding
Q	0010951	biological_process	negative regulation of endopeptidase activity
Q	0015630	cellular_component	microtubule cytoskeleton
Q	0016020	cellular_component	membrane
Q	0016241	biological_process	regulation of macroautophagy
Q	0016491	molecular_function	oxidoreductase activity
Q	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Q	0016740	molecular_function	transferase activity
Q	0017148	biological_process	negative regulation of translation
Q	0019828	molecular_function	aspartic-type endopeptidase inhibitor activity
Q	0031640	biological_process	killing of cells of another organism
Q	0031965	cellular_component	nuclear membrane
Q	0031982	cellular_component	vesicle
Q	0032481	biological_process	positive regulation of type I interferon production
Q	0035605	molecular_function	peptidyl-cysteine S-nitrosylase activity
Q	0035606	biological_process	peptidyl-cysteine S-trans-nitrosylation
Q	0042802	molecular_function	identical protein binding
Q	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
Q	0043231	cellular_component	intracellular membrane-bounded organelle
Q	0045087	biological_process	innate immune response
Q	0048471	cellular_component	perinuclear region of cytoplasm
Q	0050661	molecular_function	NADP binding
Q	0050821	biological_process	protein stabilization
Q	0050832	biological_process	defense response to fungus
Q	0051287	molecular_function	NAD binding
Q	0051402	biological_process	neuron apoptotic process
Q	0051873	biological_process	killing by host of symbiont cells
Q	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
Q	0070062	cellular_component	extracellular exosome
Q	0071346	biological_process	cellular response to type II interferon
Q	0097452	cellular_component	GAIT complex
Q	0097718	molecular_function	disordered domain specific binding
Q	1990904	cellular_component	ribonucleoprotein complex
R	0000226	biological_process	microtubule cytoskeleton organization
R	0001819	biological_process	positive regulation of cytokine production
R	0004365	molecular_function	glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity
R	0005515	molecular_function	protein binding
R	0005634	cellular_component	nucleus
R	0005737	cellular_component	cytoplasm
R	0005811	cellular_component	lipid droplet
R	0005829	cellular_component	cytosol
R	0005856	cellular_component	cytoskeleton
R	0005886	cellular_component	plasma membrane
R	0006006	biological_process	glucose metabolic process
R	0006096	biological_process	glycolytic process
R	0006417	biological_process	regulation of translation
R	0006915	biological_process	apoptotic process
R	0008017	molecular_function	microtubule binding
R	0010951	biological_process	negative regulation of endopeptidase activity
R	0015630	cellular_component	microtubule cytoskeleton
R	0016020	cellular_component	membrane
R	0016241	biological_process	regulation of macroautophagy
R	0016491	molecular_function	oxidoreductase activity
R	0016620	molecular_function	oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
R	0016740	molecular_function	transferase activity
R	0017148	biological_process	negative regulation of translation
R	0019828	molecular_function	aspartic-type endopeptidase inhibitor activity
R	0031640	biological_process	killing of cells of another organism
R	0031965	cellular_component	nuclear membrane
R	0031982	cellular_component	vesicle
R	0032481	biological_process	positive regulation of type I interferon production
R	0035605	molecular_function	peptidyl-cysteine S-nitrosylase activity
R	0035606	biological_process	peptidyl-cysteine S-trans-nitrosylation
R	0042802	molecular_function	identical protein binding
R	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
R	0043231	cellular_component	intracellular membrane-bounded organelle
R	0045087	biological_process	innate immune response
R	0048471	cellular_component	perinuclear region of cytoplasm
R	0050661	molecular_function	NADP binding
R	0050821	biological_process	protein stabilization
R	0050832	biological_process	defense response to fungus
R	0051287	molecular_function	NAD binding
R	0051402	biological_process	neuron apoptotic process
R	0051873	biological_process	killing by host of symbiont cells
R	0061844	biological_process	antimicrobial humoral immune response mediated by antimicrobial peptide
R	0070062	cellular_component	extracellular exosome
R	0071346	biological_process	cellular response to type II interferon
R	0097452	cellular_component	GAIT complex
R	0097718	molecular_function	disordered domain specific binding
R	1990904	cellular_component	ribonucleoprotein complex

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	binding site for residue EDO O 401

Chain	Residue
O	LYS162
O	VAL163
O	ASP166
O	ASN167
O	HOH543
O	HOH608

site_id	AC2
Number of Residues	4
Details	binding site for residue EDO O 402

Chain	Residue
O	HOH655
O	ASP39
O	LEU40
O	ASN41

site_id	AC3
Number of Residues	4
Details	binding site for residue PEG O 403

Chain	Residue
O	PRO129
O	MET130
O	PHE131
O	HOH582

site_id	AC4
Number of Residues	3
Details	binding site for residue ZN O 404

Chain	Residue
O	HIS57
O	HOH559
O	HOH783

site_id	AC5
Number of Residues	4
Details	binding site for residue ZN O 405

Chain	Residue
O	ASP289
O	HIS291
O	HOH598
O	HOH741

site_id	AC6
Number of Residues	13
Details	binding site for residue F4F O 406

Chain	Residue
O	PRO124
O	SER151
O	CYS152
O	THR153
O	HIS179
O	THR211
O	GLY212
O	ARG234
O	NAD407
O	HOH508
O	HOH509
O	HOH535
O	HOH563

site_id	AC7
Number of Residues	33
Details	binding site for residue NAD O 407

Chain	Residue
O	ASN9
O	GLY10
O	PHE11
O	GLY12
O	ARG13
O	ILE14
O	ASN34
O	ASP35
O	PRO36
O	PHE37
O	ARG80
O	SER98
O	THR99
O	GLY100
O	SER122
O	ALA123
O	CYS152
O	ALA183
O	ASN316
O	TYR320
O	F4F406
O	HOH530
O	HOH538
O	HOH558
O	HOH569
O	HOH591
O	HOH595
O	HOH597
O	HOH599
O	HOH616
O	HOH657
O	HOH664
O	HOH674

site_id	AC8
Number of Residues	3
Details	binding site for residue EDO Q 401

Chain	Residue
Q	PRO129
Q	MET130
Q	ASN136

site_id	AC9
Number of Residues	5
Details	binding site for residue EDO Q 402

Chain	Residue
O	HOH770
Q	GLY88
Q	ASP89
Q	GLY115
Q	HOH668

site_id	AD1
Number of Residues	5
Details	binding site for residue EDO Q 403

Chain	Residue
Q	ASP39
Q	LEU40
Q	ILE76
Q	GLN78
Q	HOH643

site_id	AD2
Number of Residues	6
Details	binding site for residue EDO Q 404

Chain	Residue
O	TYR49
Q	THR277
Q	HIS279
Q	HOH588
Q	HOH607
Q	HOH628

site_id	AD3
Number of Residues	4
Details	binding site for residue EDO Q 405

Chain	Residue
P	GLU106
Q	PRO252
Q	LYS254
Q	ASP305

site_id	AD4
Number of Residues	5
Details	binding site for residue ZN Q 406

Chain	Residue
Q	ASP289
Q	HIS291
Q	HOH588
Q	HOH651
Q	HOH735

site_id	AD5
Number of Residues	30
Details	binding site for residue NAD Q 408

Chain	Residue
Q	ARG13
Q	ILE14
Q	ASN34
Q	ASP35
Q	PRO36
Q	PHE37
Q	ARG80
Q	SER98
Q	THR99
Q	GLY100
Q	SER122
Q	ALA123
Q	CYS152
Q	ALA183
Q	ASN316
Q	TYR320
Q	F4F407
Q	HOH509
Q	HOH525
Q	HOH558
Q	HOH567
Q	HOH584
Q	HOH659
Q	HOH677
Q	HOH696
Q	HOH702
Q	ASN9
Q	GLY10
Q	PHE11
Q	GLY12

site_id	AD6
Number of Residues	4
Details	binding site for residue EDO P 401

Chain	Residue
P	THR277
P	HIS279
P	PHE286
P	HOH586

site_id	AD7
Number of Residues	5
Details	binding site for residue EDO P 402

Chain	Residue
P	ARG20
P	ASN24
P	PHE56
P	HIS57
P	PHE318

site_id	AD8
Number of Residues	3
Details	binding site for residue EDO P 403

Chain	Residue
P	LYS254
P	ASN304
P	ASP305

site_id	AD9
Number of Residues	6
Details	binding site for residue ZN P 404

Chain	Residue
O	HIS330
O	HOH528
O	HOH549
P	GLU335
P	HOH624
P	HOH666

site_id	AE1
Number of Residues	5
Details	binding site for residue ZN P 405

Chain	Residue
P	ASP289
P	HIS291
P	HOH586
P	HOH664
P	HOH721

site_id	AE2
Number of Residues	5
Details	binding site for residue EDO R 401

Chain	Residue
R	GLY300
R	ILE301
R	ALA302
R	HOH502
R	HOH605

site_id	AE3
Number of Residues	5
Details	binding site for residue GOL R 402

Chain	Residue
R	GLY193
R	LYS194
R	TRP196
R	HOH535
R	HOH606

site_id	AE4
Number of Residues	17
Details	binding site for Di-peptide F4F Q 407 and CYS Q 152

Chain	Residue
Q	PRO124
Q	SER151
Q	THR153
Q	THR154
Q	ASN155
Q	CYS156
Q	THR177
Q	HIS179
Q	THR211
Q	GLY212
Q	ALA213
Q	ARG234
Q	TYR314
Q	TYR320
Q	NAD408
Q	HOH530
Q	HOH623

Functional Information from PROSITE/UniProt

site_id	PS00071
Number of Residues	8
Details	GAPDH Glyceraldehyde 3-phosphate dehydrogenase active site. ASCTTNcL

Chain	Residue	Details
O	ALA150-LEU157

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: Nucleophile => ECO:0000269\|PubMed:25086035

Chain	Residue	Details
O	CYS152
Q	CYS152
P	CYS152
R	CYS152

site_id	SWS_FT_FI2
Number of Residues	20
Details	BINDING: BINDING => ECO:0000269\|PubMed:16239728, ECO:0000269\|PubMed:16510976

Chain	Residue	Details
O	ASN316
Q	ARG13
Q	ASP35
Q	ARG80
Q	SER122
Q	ASN316
P	ARG13
P	ASP35
P	ARG80
P	SER122
P	ASN316
R	ARG13
R	ASP35
R	ARG80
R	SER122
R	ASN316
O	ARG13
O	ASP35
O	ARG80
O	SER122

site_id	SWS_FT_FI3
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P22513

Chain	Residue	Details
R	SER151
R	THR182
R	THR211
R	ARG234
O	SER151
O	THR182
O	THR211
O	ARG234
Q	SER151
Q	THR182
Q	THR211
Q	ARG234
P	SER151
P	THR182
P	THR211
P	ARG234

site_id	SWS_FT_FI4
Number of Residues	4
Details	SITE: Activates thiol group during catalysis => ECO:0000305\|PubMed:16239728, ECO:0000305\|PubMed:16510976

Chain	Residue	Details
O	HIS179
Q	HIS179
P	HIS179
R	HIS179

site_id	SWS_FT_FI5
Number of Residues	20
Details	MOD_RES: N6,N6-dimethyllysine => ECO:0000269\|PubMed:18183946

Chain	Residue	Details
Q	LYS263
Q	LYS334
P	LYS5
P	LYS66
P	LYS260
P	LYS263
P	LYS334
R	LYS5
R	LYS66
R	LYS260
R	LYS263
R	LYS334
O	LYS5
O	LYS66
O	LYS260
O	LYS263
O	LYS334
Q	LYS5
Q	LYS66
Q	LYS260

site_id	SWS_FT_FI6
Number of Residues	28
Details	MOD_RES: Deamidated asparagine => ECO:0000269\|PubMed:18183946

Chain	Residue	Details
O	ASN155
O	ASN225
O	ASN316
Q	ASN9
Q	ASN64
Q	ASN70
Q	ASN149
Q	ASN155
Q	ASN225
Q	ASN316
P	ASN9
P	ASN64
P	ASN70
P	ASN149
P	ASN155
P	ASN225
P	ASN316
R	ASN9
R	ASN64
R	ASN70
R	ASN149
R	ASN155
R	ASN225
R	ASN316
O	ASN9
O	ASN64
O	ASN70
O	ASN149

site_id	SWS_FT_FI7
Number of Residues	4
Details	MOD_RES: Phosphotyrosine => ECO:0007744\|PubMed:15592455

Chain	Residue	Details
O	TYR42
Q	TYR42
P	TYR42
R	TYR42

site_id	SWS_FT_FI8
Number of Residues	4
Details	MOD_RES: Methionine sulfoxide; in vitro => ECO:0000305\|PubMed:25086035

Chain	Residue	Details
O	MET46
Q	MET46
P	MET46
R	MET46

site_id	SWS_FT_FI9
Number of Residues	12
Details	MOD_RES: N6-acetyllysine => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
Q	LYS219
Q	LYS254
P	LYS61
P	LYS219
P	LYS254
R	LYS61
R	LYS219
R	LYS254
O	LYS61
O	LYS219
O	LYS254
Q	LYS61

site_id	SWS_FT_FI10
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:18183946, ECO:0007744\|PubMed:20068231

Chain	Residue	Details
O	THR75
Q	THR75
P	THR75
R	THR75

site_id	SWS_FT_FI11
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:17081983, ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:21406692, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
O	SER83
Q	SER83
P	SER83
R	SER83

site_id	SWS_FT_FI12
Number of Residues	8
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:18183946

Chain	Residue	Details
P	SER122
P	SER148
R	SER122
R	SER148
O	SER148
Q	SER122
Q	SER148
O	SER122

site_id	SWS_FT_FI13
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
Q	SER151
P	SER151
R	SER151
O	SER151

site_id	SWS_FT_FI14
Number of Residues	4
Details	MOD_RES: S-nitrosocysteine; in reversibly inhibited form => ECO:0000250\|UniProtKB:P04797

Chain	Residue	Details
O	CYS152
P	CYS152
Q	CYS152
R	CYS152

site_id	SWS_FT_FI15
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
O	THR153
Q	THR153
P	THR153
R	THR153

site_id	SWS_FT_FI16
Number of Residues	8
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
P	THR177
P	THR182
R	THR177
R	THR182
O	THR177
O	THR182
Q	THR177
Q	THR182

site_id	SWS_FT_FI17
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:18669648, ECO:0007744\|PubMed:19690332, ECO:0007744\|PubMed:20068231, ECO:0007744\|PubMed:24275569

Chain	Residue	Details
O	THR184
Q	THR184
P	THR184
R	THR184

site_id	SWS_FT_FI18
Number of Residues	8
Details	MOD_RES: N6-malonyllysine; alternate => ECO:0000269\|PubMed:21908771

Chain	Residue	Details
Q	LYS194
Q	LYS215
P	LYS194
P	LYS215
O	LYS194
O	LYS215
R	LYS194
R	LYS215

site_id	SWS_FT_FI19
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0007744\|PubMed:19690332

Chain	Residue	Details
Q	THR211
P	THR211
R	THR211
O	THR211

site_id	SWS_FT_FI20
Number of Residues	4
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744\|PubMed:19608861

Chain	Residue	Details
O	LYS227
Q	LYS227
P	LYS227
R	LYS227

site_id	SWS_FT_FI21
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:18183946, ECO:0007744\|PubMed:23186163

Chain	Residue	Details
O	THR229
Q	THR229
P	THR229
R	THR229

site_id	SWS_FT_FI22
Number of Residues	4
Details	MOD_RES: Phosphothreonine => ECO:0000269\|PubMed:18183946

Chain	Residue	Details
O	THR237
Q	THR237
P	THR237
R	THR237

site_id	SWS_FT_FI23
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:24275569

Chain	Residue	Details
O	SER241
Q	SER241
P	SER241
R	SER241

site_id	SWS_FT_FI24
Number of Residues	4
Details	MOD_RES: S-nitrosocysteine => ECO:0000269\|PubMed:22771119, ECO:0000269\|PubMed:25417112

Chain	Residue	Details
O	CYS247
Q	CYS247
P	CYS247
R	CYS247

site_id	SWS_FT_FI25
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0000269\|PubMed:18183946, ECO:0007744\|PubMed:19690332

Chain	Residue	Details
O	SER312
Q	SER312
P	SER312
R	SER312

site_id	SWS_FT_FI26
Number of Residues	4
Details	MOD_RES: Phosphoserine => ECO:0007744\|PubMed:23186163

Chain	Residue	Details
O	SER333
Q	SER333
P	SER333
R	SER333

site_id	SWS_FT_FI27
Number of Residues	8
Details	CARBOHYD: (Microbial infection) N-beta-linked (GlcNAc) arginine => ECO:0000269\|PubMed:28522607

Chain	Residue	Details
P	ARG197
P	ARG200
R	ARG197
R	ARG200
O	ARG197
O	ARG200
Q	ARG197
Q	ARG200

site_id	SWS_FT_FI28
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744\|PubMed:28112733

Chain	Residue	Details
P	LYS186
R	LYS186
O	LYS186
Q	LYS186

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