Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

3N25

The structure of muscle pyruvate kinase in complex with proline, pyruvate, and Mn2+

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000287	molecular_function	magnesium ion binding
A	0003729	molecular_function	mRNA binding
A	0003824	molecular_function	catalytic activity
A	0004713	molecular_function	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	0030955	molecular_function	potassium ion binding
A	0032869	biological_process	cellular response to insulin stimulus
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	0000287	molecular_function	magnesium ion binding
B	0003729	molecular_function	mRNA binding
B	0003824	molecular_function	catalytic activity
B	0004713	molecular_function	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	0030955	molecular_function	potassium ion binding
B	0032869	biological_process	cellular response to insulin stimulus
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	0000287	molecular_function	magnesium ion binding
C	0003729	molecular_function	mRNA binding
C	0003824	molecular_function	catalytic activity
C	0004713	molecular_function	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	0030955	molecular_function	potassium ion binding
C	0032869	biological_process	cellular response to insulin stimulus
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	0000287	molecular_function	magnesium ion binding
D	0003729	molecular_function	mRNA binding
D	0003824	molecular_function	catalytic activity
D	0004713	molecular_function	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	0030955	molecular_function	potassium ion binding
D	0032869	biological_process	cellular response to insulin stimulus
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	0000287	molecular_function	magnesium ion binding
E	0003729	molecular_function	mRNA binding
E	0003824	molecular_function	catalytic activity
E	0004713	molecular_function	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	0030955	molecular_function	potassium ion binding
E	0032869	biological_process	cellular response to insulin stimulus
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	0000287	molecular_function	magnesium ion binding
F	0003729	molecular_function	mRNA binding
F	0003824	molecular_function	catalytic activity
F	0004713	molecular_function	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	0030955	molecular_function	potassium ion binding
F	0032869	biological_process	cellular response to insulin stimulus
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	0000287	molecular_function	magnesium ion binding
G	0003729	molecular_function	mRNA binding
G	0003824	molecular_function	catalytic activity
G	0004713	molecular_function	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	0030955	molecular_function	potassium ion binding
G	0032869	biological_process	cellular response to insulin stimulus
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	0000287	molecular_function	magnesium ion binding
H	0003729	molecular_function	mRNA binding
H	0003824	molecular_function	catalytic activity
H	0004713	molecular_function	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	0030955	molecular_function	potassium ion binding
H	0032869	biological_process	cellular response to insulin stimulus
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	10
Details	BINDING SITE FOR RESIDUE PRO A 1200

Chain	Residue
A	ARG42
A	HOH1265
A	ASN43
A	ASN69
A	ARG105
A	HIS463
A	TYR465
A	ILE468
A	PHE469
A	PRO470

site_id	AC2
Number of Residues	8
Details	BINDING SITE FOR RESIDUE PRO B 1600

Chain	Residue
B	ARG42
B	ASN43
B	ASN69
B	HIS463
B	ILE468
B	PHE469
B	PRO470
B	HOH769

site_id	AC3
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PRO C 1600

Chain	Residue
C	ARG42
C	ASN43
C	GLY45
C	ASN69
C	ARG105
C	HIS463
C	ILE468
C	PHE469
C	PRO470
C	HOH1638

site_id	AC4
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PRO D 1600

Chain	Residue
D	ARG42
D	ASN43
D	ASN69
D	ARG105
D	HIS463
D	ILE468
D	PHE469
D	PRO470
D	HOH1419

site_id	AC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PRO E 1600

Chain	Residue
E	ARG42
E	ASN43
E	ASN69
E	ARG105
E	HIS463
E	ILE468
E	PHE469
E	PRO470
E	HOH990
E	HOH1421

site_id	AC6
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PRO F 1600

Chain	Residue
F	ARG42
F	ASN43
F	ASN69
F	ARG105
F	HIS463
F	TYR465
F	ILE468
F	PHE469
F	PRO470
F	HOH1422
F	HOH1622

site_id	AC7
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PRO G 1600

Chain	Residue
G	ARG42
G	ASN43
G	ASN69
G	ARG105
G	HIS463
G	TYR465
G	ILE468
G	PHE469
G	PRO470
G	HOH922

site_id	AC8
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PRO H 1600

Chain	Residue
H	ARG42
H	ASN43
H	ASN69
H	ARG105
H	HIS463
H	TYR465
H	ILE468
H	PHE469
H	PRO470

site_id	AC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN A 640

Chain	Residue
A	GLU271
A	ASP295
A	PYR1000
A	HOH1225
A	HOH1275

site_id	BC1
Number of Residues	12
Details	BINDING SITE FOR RESIDUE PYR A 1000

Chain	Residue
A	ARG72
A	LYS269
A	GLU271
A	ALA292
A	ARG293
A	GLY294
A	ASP295
A	THR327
A	MN640
A	HOH1214
A	HOH1225
A	HOH1275

site_id	BC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K A 1100

Chain	Residue
A	HOH1069
A	ASN74
A	SER76
A	ASP112
A	THR113
A	HOH765

site_id	BC3
Number of Residues	6
Details	BINDING SITE FOR RESIDUE NA A 1300

Chain	Residue
A	LYS124
A	GLY125
A	SER126
A	GLY127
A	THR128
A	HOH1392

site_id	BC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE NA A 2100

Chain	Residue
A	THR431
A	SER433
A	SER436

site_id	BC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL A 6002

Chain	Residue
A	ARG42
A	LYS65
A	SER66
A	GLY67
A	HIS378

site_id	BC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO A 6043

Chain	Residue
A	GLU95
A	TYR104
A	HIS456

site_id	BC7
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO A 6050

Chain	Residue
A	GLU284
A	ALA285
A	SER286
A	ASP287
A	LYS321

site_id	BC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO A 6051

Chain	Residue
A	ARG338
A	PRO339
A	ARG341
A	HOH655
C	ASP177
C	GLN328

site_id	BC9
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL A 6201

Chain	Residue
A	PRO116
A	ASN209
A	LEU210
A	VAL215
A	PHE243
A	ARG245
A	GLU299
A	GOL6301

site_id	CC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL A 6301

Chain	Residue
A	GLU117
A	ILE118
A	GLY207
A	VAL208
A	PHE243
A	ASP295
A	GOL6201

site_id	CC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN B 640

Chain	Residue
B	GLU271
B	ASP295
B	HOH1195
B	PYR1500
B	HOH1630

site_id	CC3
Number of Residues	13
Details	BINDING SITE FOR RESIDUE PYR B 1500

Chain	Residue
B	ARG72
B	LYS269
B	GLU271
B	ALA292
B	ARG293
B	GLY294
B	ASP295
B	THR327
B	MN640
B	HOH1195
B	HOH1604
B	HOH1630
B	EDO6048

site_id	CC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K B 1700

Chain	Residue
B	ASN74
B	SER76
B	ASP112
B	THR113
B	SER242

site_id	CC5
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA B 2000

Chain	Residue
B	SER436
B	HOH1602

site_id	CC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE GOL B 6007

Chain	Residue
B	LYS65
B	SER66
B	HIS378

site_id	CC7
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO B 6013

Chain	Residue
B	ALA37
B	PRO38

site_id	CC8
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO B 6048

Chain	Residue
B	ASP177
B	ASP295
B	ILE298
B	HOH1195
B	PYR1500

site_id	CC9
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 6202

Chain	Residue
B	PRO116
B	ASN209
B	LEU210
B	VAL215
B	PHE243
B	ARG245
B	GLU299

site_id	DC1
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL B 6302

Chain	Residue
B	GLU117
B	ILE118
B	GLY207
B	VAL208
B	PHE243
B	ASP295
B	HOH1232

site_id	DC2
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN C 640

Chain	Residue
C	GLU271
C	ASP295
C	HOH1196
C	PYR1500
C	HOH1614

site_id	DC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PYR C 1500

Chain	Residue
C	LYS269
C	GLU271
C	ALA292
C	ARG293
C	GLY294
C	ASP295
C	THR327
C	MN640
C	HOH1614

site_id	DC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K C 1700

Chain	Residue
C	ASN74
C	SER76
C	ASP112
C	THR113
C	SER242
C	HOH1097

site_id	DC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA C 2000

Chain	Residue
C	THR431
C	SER433
C	SER436
C	HOH1263

site_id	DC6
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO C 6014

Chain	Residue
C	ALA37
C	PRO38
C	THR40

site_id	DC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE GOL C 6055

Chain	Residue
C	PHE97
C	LEU103
C	ARG105
C	ARG499

site_id	DC8
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL C 6303

Chain	Residue
C	GLU117
C	ILE118
C	GLY207
C	VAL208
C	PHE243
C	ASP295

site_id	DC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 6056

Chain	Residue
C	ARG391
D	ALA398
D	ARG399
D	SER402
D	HOH1038
D	HOH1610

site_id	EC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN D 640

Chain	Residue
D	GLU271
D	ASP295
D	HOH1274
D	PYR1500

site_id	EC2
Number of Residues	11
Details	BINDING SITE FOR RESIDUE PYR D 1500

Chain	Residue
D	LYS269
D	GLU271
D	ALA292
D	ARG293
D	GLY294
D	ASP295
D	THR327
D	MN640
D	HOH1274
D	HOH1625
D	EDO6033

site_id	EC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K D 1700

Chain	Residue
D	ASN74
D	SER76
D	ASP112
D	THR113
D	SER242

site_id	EC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D 2000

Chain	Residue
D	LYS124
D	GLY125
D	THR128
D	HOH1394

site_id	EC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA D 2100

Chain	Residue
D	THR431
D	SER433
D	SER436
D	HOH1395

site_id	EC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO D 6011

Chain	Residue
D	PRO38
D	THR40

site_id	EC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO D 6017

Chain	Residue
D	THR49
D	ARG72
D	ASN74
D	ALA365

site_id	EC8
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EDO D 6033

Chain	Residue
D	ASP177
D	PYR1500

site_id	EC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL D 6204

Chain	Residue
D	PRO116
D	ASN209
D	LEU210
D	VAL215
D	ARG245
D	GLU299

site_id	FC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL D 6304

Chain	Residue
D	GLU117
D	ILE118
D	VAL208
D	PHE243
D	ASP295

site_id	FC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE MN E 640

Chain	Residue
E	GLU271
E	ASP295
E	PYR1500
E	HOH1638

site_id	FC3
Number of Residues	9
Details	BINDING SITE FOR RESIDUE PYR E 1500

Chain	Residue
E	LYS269
E	GLU271
E	ALA292
E	ARG293
E	GLY294
E	ASP295
E	THR327
E	MN640
E	HOH1638

site_id	FC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE K E 1700

Chain	Residue
E	ASN74
E	SER76
E	ASP112
E	THR113
E	HOH1051

site_id	FC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA E 2000

Chain	Residue
E	LYS124
E	GLY125
E	SER126
E	GLY127
E	THR128

site_id	FC6
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA E 2100

Chain	Residue
E	THR431
E	SER433
E	SER436
E	HOH1310
E	HOH1396

site_id	FC7
Number of Residues	1
Details	BINDING SITE FOR RESIDUE EDO E 6015

Chain	Residue
E	PRO38

site_id	FC8
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EDO E 6039

Chain	Residue
E	ASP177
E	GLY294
E	HOH565

site_id	FC9
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EDO E 6046

Chain	Residue
E	ILE50
E	GLY51
E	PRO52
E	ASN74
E	ALA365
E	HOH1198

site_id	GC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO E 6049

Chain	Residue
E	ARG254
E	GLU284
E	ALA285
E	ASP287
E	LYS321

site_id	GC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE GOL E 6205

Chain	Residue
E	PRO116
E	ASN209
E	LEU210
E	VAL215
E	ARG245
E	GLU299

site_id	GC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE GOL E 6305

Chain	Residue
E	GLU117
E	ILE118
E	VAL208
E	PHE243
E	ASP295

site_id	GC4
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN F 640

Chain	Residue
F	GLU271
F	ASP295
F	HOH1199
F	PYR1500
F	HOH1624

site_id	GC5
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PYR F 1500

Chain	Residue
F	LYS269
F	GLU271
F	ALA292
F	ARG293
F	GLY294
F	ASP295
F	THR327
F	MN640
F	HOH668
F	HOH1199

site_id	GC6
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K F 1700

Chain	Residue
F	ASN74
F	SER76
F	ASP112
F	THR113
F	SER242
F	HOH1656

site_id	GC7
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA F 2000

Chain	Residue
F	THR431
F	SER433
F	SER436
F	HOH1339

site_id	GC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL F 6010

Chain	Residue
F	ASP177
F	GLN328
F	HOH572
F	HOH744
H	ARG338
H	PRO339
H	THR340
H	ARG341

site_id	GC9
Number of Residues	4
Details	BINDING SITE FOR RESIDUE EDO F 6012

Chain	Residue
F	ALA37
F	PRO38
F	THR40
F	ARG382

site_id	HC1
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL F 6206

Chain	Residue
F	PRO116
F	VAL208
F	ASN209
F	LEU210
F	VAL215
F	PHE243
F	ARG245
F	GLU299

site_id	HC2
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL F 6306

Chain	Residue
F	GLU117
F	ILE118
F	GLY207
F	VAL208
F	PHE243
F	ASP295
F	HOH1624

site_id	HC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN G 640

Chain	Residue
G	GLU271
G	ASP295
G	HOH1201
G	HOH1408
G	PYR1500

site_id	HC4
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PYR G 1500

Chain	Residue
G	LYS269
G	GLU271
G	ALA292
G	ARG293
G	GLY294
G	ASP295
G	THR327
G	MN640
G	HOH651
G	HOH1408

site_id	HC5
Number of Residues	7
Details	BINDING SITE FOR RESIDUE K G 1700

Chain	Residue
G	ASN74
G	SER76
G	ASP112
G	THR113
G	SER242
G	HOH651
G	HOH1409

site_id	HC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE NA G 2000

Chain	Residue
G	THR431
G	SER436

site_id	HC7
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL G 6207

Chain	Residue
G	PRO116
G	ASN209
G	LEU210
G	VAL215
G	PHE243
G	ARG245
G	GLU299
G	GOL6307

site_id	HC8
Number of Residues	8
Details	BINDING SITE FOR RESIDUE GOL G 6307

Chain	Residue
G	GLU117
G	ILE118
G	GLY207
G	VAL208
G	PHE243
G	ASP295
G	HOH1201
G	GOL6207

site_id	HC9
Number of Residues	5
Details	BINDING SITE FOR RESIDUE MN H 640

Chain	Residue
H	GLU271
H	ASP295
H	HOH1202
H	PYR1500
H	HOH1607

site_id	IC1
Number of Residues	10
Details	BINDING SITE FOR RESIDUE PYR H 1500

Chain	Residue
H	LYS269
H	GLU271
H	ALA292
H	ARG293
H	GLY294
H	ASP295
H	THR327
H	MN640
H	HOH1202
H	HOH1607

site_id	IC2
Number of Residues	6
Details	BINDING SITE FOR RESIDUE K H 1700

Chain	Residue
H	ASN74
H	SER76
H	ASP112
H	THR113
H	HOH1064
H	HOH1418

site_id	IC3
Number of Residues	5
Details	BINDING SITE FOR RESIDUE NA H 2000

Chain	Residue
H	LYS124
H	GLY125
H	SER126
H	GLY127
H	THR128

site_id	IC4
Number of Residues	4
Details	BINDING SITE FOR RESIDUE NA H 2100

Chain	Residue
H	THR431
H	SER433
H	SER436
H	HOH1397

site_id	IC5
Number of Residues	5
Details	BINDING SITE FOR RESIDUE EDO H 6037

Chain	Residue
H	GLU284
H	ALA285
H	SER286
H	ASP287
H	LYS321

site_id	IC6
Number of Residues	7
Details	BINDING SITE FOR RESIDUE GOL H 6308

Chain	Residue
H	GLU117
H	ILE118
H	GLY207
H	VAL208
H	PHE243
H	ASP295
H	HOH1202

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	112
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
A	ASN69
A	THR431
H	ASN74
H	SER76
H	ARG105
H	ASP112
H	THR113
H	ARG119
H	LYS206
H	GLU271
H	THR431
H	HIS463
A	HIS463
H	TRP481
H	ARG488
H	ARG515
A	TRP481
A	ARG488
A	ARG515
B	ASN69
B	ASN74
B	SER76
B	ARG105
B	ASP112
A	ASN74
B	THR113
B	ARG119
B	LYS206
B	GLU271
B	THR431
B	HIS463
B	TRP481
B	ARG488
B	ARG515
C	ASN69
A	SER76
C	ASN74
C	SER76
C	ARG105
C	ASP112
C	THR113
C	ARG119
C	LYS206
C	GLU271
C	THR431
C	HIS463
A	ARG105
C	TRP481
C	ARG488
C	ARG515
D	ASN69
D	ASN74
D	SER76
D	ARG105
D	ASP112
D	THR113
D	ARG119
A	ASP112
D	LYS206
D	GLU271
D	THR431
D	HIS463
D	TRP481
D	ARG488
D	ARG515
E	ASN69
E	ASN74
E	SER76
A	THR113
E	ARG105
E	ASP112
E	THR113
E	ARG119
E	LYS206
E	GLU271
E	THR431
E	HIS463
E	TRP481
E	ARG488
A	ARG119
E	ARG515
F	ASN69
F	ASN74
F	SER76
F	ARG105
F	ASP112
F	THR113
F	ARG119
F	LYS206
F	GLU271
A	LYS206
F	THR431
F	HIS463
F	TRP481
F	ARG488
F	ARG515
G	ASN69
G	ASN74
G	SER76
G	ARG105
G	ASP112
A	GLU271
G	THR113
G	ARG119
G	LYS206
G	GLU271
G	THR431
G	HIS463
G	TRP481
G	ARG488
G	ARG515
H	ASN69

site_id	SWS_FT_FI2
Number of Residues	40
Details	BINDING: BINDING => ECO:0000250\|UniProtKB:P30613

Chain	Residue	Details
A	ARG72
B	THR327
C	ARG72
C	LYS269
C	GLY294
C	ASP295
C	THR327
D	ARG72
D	LYS269
D	GLY294
D	ASP295
A	LYS269
D	THR327
E	ARG72
E	LYS269
E	GLY294
E	ASP295
E	THR327
F	ARG72
F	LYS269
F	GLY294
F	ASP295
A	GLY294
F	THR327
G	ARG72
G	LYS269
G	GLY294
G	ASP295
G	THR327
H	ARG72
H	LYS269
H	GLY294
H	ASP295
A	ASP295
H	THR327
A	THR327
B	ARG72
B	LYS269
B	GLY294
B	ASP295

site_id	SWS_FT_FI3
Number of Residues	8
Details	SITE: Transition state stabilizer => ECO:0000250\|UniProtKB:P00549

Chain	Residue	Details
A	LYS269
B	LYS269
C	LYS269
D	LYS269
E	LYS269
F	LYS269
G	LYS269
H	LYS269

site_id	SWS_FT_FI4
Number of Residues	8
Details	MOD_RES: N-acetylserine => ECO:0000250\|UniProtKB:P11979

Chain	Residue	Details
A	SER1
B	SER1
C	SER1
D	SER1
E	SER1
F	SER1
G	SER1
H	SER1

site_id	SWS_FT_FI5
Number of Residues	8
Details	MOD_RES: N6,N6,N6-trimethyllysine => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
A	LYS2
B	LYS2
C	LYS2
D	LYS2
E	LYS2
F	LYS2
G	LYS2
H	LYS2

site_id	SWS_FT_FI6
Number of Residues	16
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
A	SER36
E	SER126
F	SER36
F	SER126
G	SER36
G	SER126
H	SER36
H	SER126
A	SER126
B	SER36
B	SER126
C	SER36
C	SER126
D	SER36
D	SER126
E	SER36

site_id	SWS_FT_FI7
Number of Residues	16
Details	MOD_RES: Phosphothreonine => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
A	THR40
E	THR194
F	THR40
F	THR194
G	THR40
G	THR194
H	THR40
H	THR194
A	THR194
B	THR40
B	THR194
C	THR40
C	THR194
D	THR40
D	THR194
E	THR40

site_id	SWS_FT_FI8
Number of Residues	24
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
A	LYS61
D	LYS61
D	LYS88
D	LYS304
E	LYS61
E	LYS88
E	LYS304
F	LYS61
F	LYS88
F	LYS304
G	LYS61
A	LYS88
G	LYS88
G	LYS304
H	LYS61
H	LYS88
H	LYS304
A	LYS304
B	LYS61
B	LYS88
B	LYS304
C	LYS61
C	LYS88
C	LYS304

site_id	SWS_FT_FI9
Number of Residues	16
Details	MOD_RES: N6-succinyllysine => ECO:0000250\|UniProtKB:P52480

Chain	Residue	Details
A	LYS65
E	LYS497
F	LYS65
F	LYS497
G	LYS65
G	LYS497
H	LYS65
H	LYS497
A	LYS497
B	LYS65
B	LYS497
C	LYS65
C	LYS497
D	LYS65
D	LYS497
E	LYS65

site_id	SWS_FT_FI10
Number of Residues	16
Details	MOD_RES: Phosphoserine => ECO:0000250\|UniProtKB:P11980

Chain	Residue	Details
A	SER96
E	SER99
F	SER96
F	SER99
G	SER96
G	SER99
H	SER96
H	SER99
A	SER99
B	SER96
B	SER99
C	SER96
C	SER99
D	SER96
D	SER99
E	SER96

site_id	SWS_FT_FI11
Number of Residues	16
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
A	TYR104
E	TYR174
F	TYR104
F	TYR174
G	TYR104
G	TYR174
H	TYR104
H	TYR174
A	TYR174
B	TYR104
B	TYR174
C	TYR104
C	TYR174
D	TYR104
D	TYR174
E	TYR104

site_id	SWS_FT_FI12
Number of Residues	8
Details	MOD_RES: Phosphotyrosine => ECO:0000250\|UniProtKB:P52480

Chain	Residue	Details
A	TYR147
B	TYR147
C	TYR147
D	TYR147
E	TYR147
F	TYR147
G	TYR147
H	TYR147

site_id	SWS_FT_FI13
Number of Residues	16
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250\|UniProtKB:P52480

Chain	Residue	Details
A	LYS165
E	LYS321
F	LYS165
F	LYS321
G	LYS165
G	LYS321
H	LYS165
H	LYS321
A	LYS321
B	LYS165
B	LYS321
C	LYS165
C	LYS321
D	LYS165
D	LYS321
E	LYS165

site_id	SWS_FT_FI14
Number of Residues	8
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
A	LYS265
B	LYS265
C	LYS265
D	LYS265
E	LYS265
F	LYS265
G	LYS265
H	LYS265

site_id	SWS_FT_FI15
Number of Residues	8
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250\|UniProtKB:P52480

Chain	Residue	Details
A	LYS269
B	LYS269
C	LYS269
D	LYS269
E	LYS269
F	LYS269
G	LYS269
H	LYS269

site_id	SWS_FT_FI16
Number of Residues	8
Details	MOD_RES: N6-acetyllysine => ECO:0000250\|UniProtKB:P52480

Chain	Residue	Details
A	LYS474
B	LYS474
C	LYS474
D	LYS474
E	LYS474
F	LYS474
G	LYS474
H	LYS474

site_id	SWS_FT_FI17
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
A	LYS114
B	LYS114
C	LYS114
D	LYS114
E	LYS114
F	LYS114
G	LYS114
H	LYS114

site_id	SWS_FT_FI18
Number of Residues	24
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
D	LYS265
D	LYS269
E	LYS265
E	LYS269
F	LYS265
F	LYS269
A	LYS265
G	LYS265
G	LYS269
H	LYS265
H	LYS269
A	LYS269
B	LYS265
B	LYS269
C	LYS265
C	LYS269

site_id	SWS_FT_FI19
Number of Residues	8
Details	CROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternate => ECO:0000250\|UniProtKB:P14618

Chain	Residue	Details
A	LYS165
B	LYS165
C	LYS165
D	LYS165
E	LYS165
F	LYS165
G	LYS165
H	LYS165

Catalytic Information from CSA

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	ARG72	attractive charge-charge interaction, electrostatic stabiliser, steric role
B	ARG119	attractive charge-charge interaction, electrostatic stabiliser, steric role
B	LYS269	attractive charge-charge interaction, electrostatic stabiliser, hydrogen bond donor, steric role
B	THR327	electrostatic stabiliser, hydrogen bond donor, increase acidity

site_id	MCSA3
Number of Residues	4
Details	M-CSA 326

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

site_id	MCSA4
Number of Residues	4
Details	M-CSA 326

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

site_id	MCSA5
Number of Residues	4
Details	M-CSA 326

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

site_id	MCSA6
Number of Residues	4
Details	M-CSA 326

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

site_id	MCSA7
Number of Residues	4
Details	M-CSA 326

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

site_id	MCSA8
Number of Residues	4
Details	M-CSA 326

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

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