Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

1A49

BIS MG-ATP-K-OXALATE COMPLEX OF PYRUVATE KINASE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0003729	molecular_function	mRNA binding
A	0003824	molecular_function	catalytic activity
A	0004674	molecular_function	protein serine/threonine kinase activity
A	0004713	molecular_function	protein tyrosine kinase activity
A	0004715	molecular_function	non-membrane spanning protein tyrosine kinase activity
A	0004743	molecular_function	pyruvate kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005634	cellular_component	nucleus
A	0005737	cellular_component	cytoplasm
A	0005791	cellular_component	rough endoplasmic reticulum
A	0006096	biological_process	glycolytic process
A	0006417	biological_process	regulation of translation
A	0016301	molecular_function	kinase activity
A	0016740	molecular_function	transferase activity
A	0030955	molecular_function	potassium ion binding
A	0046872	molecular_function	metal ion binding
A	1903672	biological_process	positive regulation of sprouting angiogenesis
A	2000767	biological_process	positive regulation of cytoplasmic translation
B	0000166	molecular_function	nucleotide binding
B	0000287	molecular_function	magnesium ion binding
B	0003729	molecular_function	mRNA binding
B	0003824	molecular_function	catalytic activity
B	0004674	molecular_function	protein serine/threonine kinase activity
B	0004713	molecular_function	protein tyrosine kinase activity
B	0004715	molecular_function	non-membrane spanning protein tyrosine kinase activity
B	0004743	molecular_function	pyruvate kinase activity
B	0005515	molecular_function	protein binding
B	0005524	molecular_function	ATP binding
B	0005634	cellular_component	nucleus
B	0005737	cellular_component	cytoplasm
B	0005791	cellular_component	rough endoplasmic reticulum
B	0006096	biological_process	glycolytic process
B	0006417	biological_process	regulation of translation
B	0016301	molecular_function	kinase activity
B	0016740	molecular_function	transferase activity
B	0030955	molecular_function	potassium ion binding
B	0046872	molecular_function	metal ion binding
B	1903672	biological_process	positive regulation of sprouting angiogenesis
B	2000767	biological_process	positive regulation of cytoplasmic translation
C	0000166	molecular_function	nucleotide binding
C	0000287	molecular_function	magnesium ion binding
C	0003729	molecular_function	mRNA binding
C	0003824	molecular_function	catalytic activity
C	0004674	molecular_function	protein serine/threonine kinase activity
C	0004713	molecular_function	protein tyrosine kinase activity
C	0004715	molecular_function	non-membrane spanning protein tyrosine kinase activity
C	0004743	molecular_function	pyruvate kinase activity
C	0005515	molecular_function	protein binding
C	0005524	molecular_function	ATP binding
C	0005634	cellular_component	nucleus
C	0005737	cellular_component	cytoplasm
C	0005791	cellular_component	rough endoplasmic reticulum
C	0006096	biological_process	glycolytic process
C	0006417	biological_process	regulation of translation
C	0016301	molecular_function	kinase activity
C	0016740	molecular_function	transferase activity
C	0030955	molecular_function	potassium ion binding
C	0046872	molecular_function	metal ion binding
C	1903672	biological_process	positive regulation of sprouting angiogenesis
C	2000767	biological_process	positive regulation of cytoplasmic translation
D	0000166	molecular_function	nucleotide binding
D	0000287	molecular_function	magnesium ion binding
D	0003729	molecular_function	mRNA binding
D	0003824	molecular_function	catalytic activity
D	0004674	molecular_function	protein serine/threonine kinase activity
D	0004713	molecular_function	protein tyrosine kinase activity
D	0004715	molecular_function	non-membrane spanning protein tyrosine kinase activity
D	0004743	molecular_function	pyruvate kinase activity
D	0005515	molecular_function	protein binding
D	0005524	molecular_function	ATP binding
D	0005634	cellular_component	nucleus
D	0005737	cellular_component	cytoplasm
D	0005791	cellular_component	rough endoplasmic reticulum
D	0006096	biological_process	glycolytic process
D	0006417	biological_process	regulation of translation
D	0016301	molecular_function	kinase activity
D	0016740	molecular_function	transferase activity
D	0030955	molecular_function	potassium ion binding
D	0046872	molecular_function	metal ion binding
D	1903672	biological_process	positive regulation of sprouting angiogenesis
D	2000767	biological_process	positive regulation of cytoplasmic translation
E	0000166	molecular_function	nucleotide binding
E	0000287	molecular_function	magnesium ion binding
E	0003729	molecular_function	mRNA binding
E	0003824	molecular_function	catalytic activity
E	0004674	molecular_function	protein serine/threonine kinase activity
E	0004713	molecular_function	protein tyrosine kinase activity
E	0004715	molecular_function	non-membrane spanning protein tyrosine kinase activity
E	0004743	molecular_function	pyruvate kinase activity
E	0005515	molecular_function	protein binding
E	0005524	molecular_function	ATP binding
E	0005634	cellular_component	nucleus
E	0005737	cellular_component	cytoplasm
E	0005791	cellular_component	rough endoplasmic reticulum
E	0006096	biological_process	glycolytic process
E	0006417	biological_process	regulation of translation
E	0016301	molecular_function	kinase activity
E	0016740	molecular_function	transferase activity
E	0030955	molecular_function	potassium ion binding
E	0046872	molecular_function	metal ion binding
E	1903672	biological_process	positive regulation of sprouting angiogenesis
E	2000767	biological_process	positive regulation of cytoplasmic translation
F	0000166	molecular_function	nucleotide binding
F	0000287	molecular_function	magnesium ion binding
F	0003729	molecular_function	mRNA binding
F	0003824	molecular_function	catalytic activity
F	0004674	molecular_function	protein serine/threonine kinase activity
F	0004713	molecular_function	protein tyrosine kinase activity
F	0004715	molecular_function	non-membrane spanning protein tyrosine kinase activity
F	0004743	molecular_function	pyruvate kinase activity
F	0005515	molecular_function	protein binding
F	0005524	molecular_function	ATP binding
F	0005634	cellular_component	nucleus
F	0005737	cellular_component	cytoplasm
F	0005791	cellular_component	rough endoplasmic reticulum
F	0006096	biological_process	glycolytic process
F	0006417	biological_process	regulation of translation
F	0016301	molecular_function	kinase activity
F	0016740	molecular_function	transferase activity
F	0030955	molecular_function	potassium ion binding
F	0046872	molecular_function	metal ion binding
F	1903672	biological_process	positive regulation of sprouting angiogenesis
F	2000767	biological_process	positive regulation of cytoplasmic translation
G	0000166	molecular_function	nucleotide binding
G	0000287	molecular_function	magnesium ion binding
G	0003729	molecular_function	mRNA binding
G	0003824	molecular_function	catalytic activity
G	0004674	molecular_function	protein serine/threonine kinase activity
G	0004713	molecular_function	protein tyrosine kinase activity
G	0004715	molecular_function	non-membrane spanning protein tyrosine kinase activity
G	0004743	molecular_function	pyruvate kinase activity
G	0005515	molecular_function	protein binding
G	0005524	molecular_function	ATP binding
G	0005634	cellular_component	nucleus
G	0005737	cellular_component	cytoplasm
G	0005791	cellular_component	rough endoplasmic reticulum
G	0006096	biological_process	glycolytic process
G	0006417	biological_process	regulation of translation
G	0016301	molecular_function	kinase activity
G	0016740	molecular_function	transferase activity
G	0030955	molecular_function	potassium ion binding
G	0046872	molecular_function	metal ion binding
G	1903672	biological_process	positive regulation of sprouting angiogenesis
G	2000767	biological_process	positive regulation of cytoplasmic translation
H	0000166	molecular_function	nucleotide binding
H	0000287	molecular_function	magnesium ion binding
H	0003729	molecular_function	mRNA binding
H	0003824	molecular_function	catalytic activity
H	0004674	molecular_function	protein serine/threonine kinase activity
H	0004713	molecular_function	protein tyrosine kinase activity
H	0004715	molecular_function	non-membrane spanning protein tyrosine kinase activity
H	0004743	molecular_function	pyruvate kinase activity
H	0005515	molecular_function	protein binding
H	0005524	molecular_function	ATP binding
H	0005634	cellular_component	nucleus
H	0005737	cellular_component	cytoplasm
H	0005791	cellular_component	rough endoplasmic reticulum
H	0006096	biological_process	glycolytic process
H	0006417	biological_process	regulation of translation
H	0016301	molecular_function	kinase activity
H	0016740	molecular_function	transferase activity
H	0030955	molecular_function	potassium ion binding
H	0046872	molecular_function	metal ion binding
H	1903672	biological_process	positive regulation of sprouting angiogenesis
H	2000767	biological_process	positive regulation of cytoplasmic translation

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 532

Chain	Residue
A	ASN74
A	SER76
A	ASP112
A	THR113
A	SER242
A	ATP535

site_id	AC2
Number of Residues	12
Details	BINDING SITE FOR RESIDUE OXL A 533

Chain	Residue
A	MET290
A	ALA292
A	ARG293
A	GLY294
A	ASP295
A	THR327
A	MG534
A	ATP535
A	HOH6763
A	ARG72
A	LYS269
A	GLU271

site_id	AC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG A 534

Chain	Residue
A	GLU271
A	ASP295
A	OXL533
A	ATP535
A	HOH6763

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE MG A 536

Chain	Residue
A	ATP535
A	HOH6079
A	HOH6469

site_id	AC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K B 1132

Chain	Residue
B	ASN674
B	SER676
B	ASP712
B	THR713
B	HOH6141

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE OXL B 1133

Chain	Residue
B	LYS869
B	GLU871
B	MET890
B	ALA892
B	ARG893
B	GLY894
B	ASP895
B	THR927
B	MG1134
B	HOH6624
B	HOH7031

site_id	AC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG B 1134

Chain	Residue
B	GLU871
B	ASP895
B	OXL1133
B	HOH7031

site_id	AC8
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K C 1732

Chain	Residue
C	ASN1274
C	SER1276
C	ASP1312
C	THR1313
C	SER1442
C	ATP1735
C	HOH7921

site_id	AC9
Number of Residues	11
Details	BINDING SITE FOR RESIDUE OXL C 1733

Chain	Residue
C	ARG1272
C	LYS1469
C	GLU1471
C	ALA1492
C	ARG1493
C	GLY1494
C	ASP1495
C	THR1527
C	MG1734
C	ATP1735
C	HOH6663

site_id	BC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG C 1734

Chain	Residue
C	LYS1469
C	GLU1471
C	ASP1495
C	OXL1733
C	ATP1735

site_id	BC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG C 1736

Chain	Residue
C	ATP1735
C	HOH6006
C	HOH6581
C	HOH6663

site_id	BC3
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K D 2332

Chain	Residue
D	ASN1874
D	SER1876
D	ASP1912
D	THR1913
D	SER2042
D	ATP2335
D	HOH7499

site_id	BC4
Number of Residues	13
Details	BINDING SITE FOR RESIDUE OXL D 2333

Chain	Residue
D	LYS2069
D	GLU2071
D	MET2090
D	ALA2092
D	ARG2093
D	GLY2094
D	ASP2095
D	THR2127
D	MET2159
D	MG2334
D	ATP2335
D	HOH6045
D	HOH6387

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG D 2334

Chain	Residue
D	GLU2071
D	ASP2095
D	OXL2333
D	ATP2335
D	HOH6439

site_id	BC6
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG D 2336

Chain	Residue
D	HOH6045
D	HOH6387
D	HOH7364
D	ATP2335

site_id	BC7
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K E 3532

Chain	Residue
E	ASN3074
E	SER3076
E	ASP3112
E	THR3113
E	SER3242
E	ATP3535
E	HOH7785

site_id	BC8
Number of Residues	12
Details	BINDING SITE FOR RESIDUE OXL E 3533

Chain	Residue
E	LYS3269
E	GLU3271
E	ALA3292
E	ARG3293
E	GLY3294
E	ASP3295
E	THR3327
E	MG3534
E	ATP3535
E	HOH6162
E	HOH6348
E	HOH6988

site_id	BC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG E 3534

Chain	Residue
E	GLU3271
E	ASP3295
E	OXL3533
E	ATP3535
E	HOH6988

site_id	CC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG E 3536

Chain	Residue
E	ATP3535
E	HOH6162
E	HOH6348
E	HOH7443

site_id	CC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K F 4132

Chain	Residue
F	ASN3674
F	SER3676
F	ASP3712
F	THR3713
F	SER3842
F	ATP4135
F	HOH6491

site_id	CC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE OXL F 4133

Chain	Residue
F	ARG3672
F	LYS3869
F	GLU3871
F	MET3890
F	ALA3892
F	ARG3893
F	GLY3894
F	ASP3895
F	THR3927
F	MG4134
F	ATP4135
F	HOH6300
F	HOH6460

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG F 4134

Chain	Residue
F	GLU3871
F	ASP3895
F	OXL4133
F	ATP4135
F	HOH6460

site_id	CC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG F 4136

Chain	Residue
F	ATP4135
F	HOH6300
F	HOH7054
F	HOH7055

site_id	CC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K G 4732

Chain	Residue
G	ASN4274
G	SER4276
G	ASP4312
G	THR4313
G	SER4442
G	ATP4735
G	HOH7049

site_id	CC7
Number of Residues	12
Details	BINDING SITE FOR RESIDUE OXL G 4733

Chain	Residue
G	ARG4272
G	LYS4469
G	GLU4471
G	ALA4492
G	ARG4493
G	GLY4494
G	ASP4495
G	THR4527
G	MG4734
G	ATP4735
G	HOH6349
G	HOH6671

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MG G 4734

Chain	Residue
G	GLU4471
G	ASP4495
G	OXL4733
G	ATP4735
G	HOH6671

site_id	CC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MG G 4736

Chain	Residue
G	ATP4735
G	HOH6177
G	HOH6256
G	HOH6349

site_id	DC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K H 5332

Chain	Residue
H	ASN4874
H	SER4876
H	ASP4912
H	THR4913
H	HOH6838
H	HOH6965

site_id	DC2
Number of Residues	10
Details	BINDING SITE FOR RESIDUE OXL H 5333

Chain	Residue
H	LYS5069
H	GLU5071
H	MET5090
H	ALA5092
H	ARG5093
H	GLY5094
H	ASP5095
H	THR5127
H	MG5334
H	HOH7293

site_id	DC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG H 5334

Chain	Residue
H	LYS5069
H	GLU5071
H	ASP5095
H	OXL5333
H	HOH7292
H	HOH7293

site_id	DC4
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP A 535

Chain	Residue
A	PRO52
A	ARG72
A	ASN74
A	HIS77
A	TYR82
A	HIS83
A	ARG119
A	LYS206
A	ASP295
A	SER361
A	LYS366
A	K532
A	OXL533
A	MG534
A	MG536
A	HOH6003
A	HOH6079
A	HOH6366
A	HOH6469
A	HOH6995
A	HOH7738
A	HOH7743

site_id	DC5
Number of Residues	22
Details	BINDING SITE FOR RESIDUE ATP C 1735

Chain	Residue
C	THR1249
C	PRO1252
C	ARG1272
C	ASN1274
C	HIS1277
C	TYR1282
C	HIS1283
C	ARG1319
C	LYS1406
C	ASP1495
C	SER1561
C	LYS1566
C	K1732
C	OXL1733
C	MG1734
C	MG1736
C	HOH6005
C	HOH6006
C	HOH6581
C	HOH6663
C	HOH6879
C	HOH7844

site_id	DC6
Number of Residues	24
Details	BINDING SITE FOR RESIDUE ATP D 2335

Chain	Residue
D	THR1849
D	PRO1852
D	ARG1872
D	ASN1874
D	HIS1877
D	TYR1882
D	ARG1919
D	LYS2006
D	ASP2095
D	SER2161
D	LYS2166
D	K2332
D	OXL2333
D	MG2334
D	MG2336
D	HOH6004
D	HOH6045
D	HOH6082
D	HOH6140
D	HOH6387
D	HOH6463
D	HOH6745
D	HOH7364
D	HOH7874

site_id	DC7
Number of Residues	26
Details	BINDING SITE FOR RESIDUE ATP E 3535

Chain	Residue
E	THR3049
E	PRO3052
E	ARG3072
E	ASN3074
E	HIS3077
E	TYR3082
E	HIS3083
E	ARG3119
E	LYS3206
E	ASP3295
E	SER3361
E	ALA3365
E	LYS3366
E	K3532
E	OXL3533
E	MG3534
E	MG3536
E	HOH6159
E	HOH6162
E	HOH6222
E	HOH6318
E	HOH6348
E	HOH6498
E	HOH7137
E	HOH7443
E	HOH7793

site_id	DC8
Number of Residues	21
Details	BINDING SITE FOR RESIDUE ATP F 4135

Chain	Residue
F	PRO3652
F	ARG3672
F	ASN3674
F	HIS3677
F	TYR3682
F	ARG3719
F	LYS3869
F	ASP3895
F	SER3961
F	LYS3966
F	K4132
F	OXL4133
F	MG4134
F	MG4136
F	HOH6178
F	HOH6300
F	HOH6460
F	HOH7054
F	HOH7055
F	HOH7453
F	HOH7923

site_id	DC9
Number of Residues	27
Details	BINDING SITE FOR RESIDUE ATP G 4735

Chain	Residue
G	THR4249
G	PRO4252
G	ARG4272
G	ASN4274
G	HIS4277
G	TYR4282
G	HIS4283
G	ARG4319
G	LYS4406
G	ASP4495
G	SER4561
G	GLY4562
G	ALA4565
G	K4732
G	OXL4733
G	MG4734
G	MG4736
G	HOH6177
G	HOH6179
G	HOH6256
G	HOH6349
G	HOH6534
G	HOH6637
G	HOH6671
G	HOH7330
G	HOH7663
G	HOH7924

Functional Information from PROSITE/UniProt

site_id	PS00110
Number of Residues	13
Details	PYRUVATE_KINASE Pyruvate kinase active site signature. IkIISKIENhEGV

Chain	Residue	Details
A	ILE264-VAL276

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1792
Details	Region: {"description":"Interaction with POU5F1","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	200
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	40
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P30613","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	8
Details	Site: {"description":"Transition state stabilizer","evidences":[{"source":"UniProtKB","id":"P00549","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	16
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	16
Details	Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	24
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	16
Details	Modified residue: {"description":"N6-succinyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	16
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P11980","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	16
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	8
Details	Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	16
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	8
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P52480","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	24
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	8
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	16
Details	Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"UniProtKB","id":"P14618","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

Catalytic Information from CSA

site_id	CSA1
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
A	LYS269
A	SER361
A	ARG119
A	GLU363
A	ARG72
A	THR327

site_id	CSA2
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
B	LYS869
B	ARG719
B	ARG672
B	THR927
B	SER961
B	GLU963

site_id	CSA3
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
C	ARG1319
C	SER1561
C	LYS1469
C	GLU1563
C	THR1527
C	ARG1272

site_id	CSA4
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
D	SER2161
D	ARG1919
D	GLU2163
D	THR2127
D	ARG1872
D	LYS2069

site_id	CSA5
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
E	GLU3363
E	THR3327
E	ARG3072
E	SER3361
E	ARG3119
E	LYS3269

site_id	CSA6
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
F	LYS3869
F	THR3927
F	SER3961
F	ARG3672
F	GLU3963
F	ARG3719

site_id	CSA7
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
G	ARG4319
G	SER4561
G	GLU4563
G	LYS4469
G	ARG4272
G	THR4527

site_id	CSA8
Number of Residues	6
Details	Annotated By Reference To The Literature 1pkn

Chain	Residue	Details
H	SER5161
H	ARG4919
H	GLU5163
H	THR5127
H	LYS5069
H	ARG4872

site_id	MCSA1
Number of Residues	4
Details	M-CSA 326

Chain	Residue	Details
A	ARG72	attractive charge-charge interaction, electrostatic stabiliser, steric role
A	ARG119	attractive charge-charge interaction, electrostatic stabiliser, steric role
A	LYS269	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
A	THR327	electrostatic stabiliser, hydrogen bond donor, increase acidity

site_id	MCSA2
Number of Residues	4
Details	M-CSA 326

Chain	Residue	Details
B	ARG672	attractive charge-charge interaction, electrostatic stabiliser, steric role
B	ARG719	attractive charge-charge interaction, electrostatic stabiliser, steric role
B	LYS869	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
B	THR927	electrostatic stabiliser, hydrogen bond donor, increase acidity

site_id	MCSA3
Number of Residues	4
Details	M-CSA 326

Chain	Residue	Details
C	ARG1272	attractive charge-charge interaction, electrostatic stabiliser, steric role
C	ARG1319	attractive charge-charge interaction, electrostatic stabiliser, steric role
C	LYS1469	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
C	THR1527	electrostatic stabiliser, hydrogen bond donor, increase acidity

site_id	MCSA4
Number of Residues	4
Details	M-CSA 326

Chain	Residue	Details
D	ARG1872	attractive charge-charge interaction, electrostatic stabiliser, steric role
D	ARG1919	attractive charge-charge interaction, electrostatic stabiliser, steric role
D	LYS2069	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
D	THR2127	electrostatic stabiliser, hydrogen bond donor, increase acidity

site_id	MCSA5
Number of Residues	4
Details	M-CSA 326

Chain	Residue	Details
E	ARG3072	attractive charge-charge interaction, electrostatic stabiliser, steric role
E	ARG3119	attractive charge-charge interaction, electrostatic stabiliser, steric role
E	LYS3269	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
E	THR3327	electrostatic stabiliser, hydrogen bond donor, increase acidity

site_id	MCSA6
Number of Residues	4
Details	M-CSA 326

Chain	Residue	Details
F	ARG3672	attractive charge-charge interaction, electrostatic stabiliser, steric role
F	ARG3719	attractive charge-charge interaction, electrostatic stabiliser, steric role
F	LYS3869	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
F	THR3927	electrostatic stabiliser, hydrogen bond donor, increase acidity

site_id	MCSA7
Number of Residues	4
Details	M-CSA 326

Chain	Residue	Details
G	ARG4272	attractive charge-charge interaction, electrostatic stabiliser, steric role
G	ARG4319	attractive charge-charge interaction, electrostatic stabiliser, steric role
G	LYS4469	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
G	THR4527	electrostatic stabiliser, hydrogen bond donor, increase acidity

site_id	MCSA8
Number of Residues	4
Details	M-CSA 326

Chain	Residue	Details
H	ARG4872	attractive charge-charge interaction, electrostatic stabiliser, steric role
H	ARG4919	attractive charge-charge interaction, electrostatic stabiliser, steric role
H	LYS5069	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
H	THR5127	electrostatic stabiliser, hydrogen bond donor, increase acidity

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)