5MXM

The X-ray structure of human M190I phosphoglycerate kinase 1 mutant

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004618	molecular_function	phosphoglycerate kinase activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016020	cellular_component	membrane
A	0016301	molecular_function	kinase activity
A	0016310	biological_process	phosphorylation
A	0016525	biological_process	negative regulation of angiogenesis
A	0030855	biological_process	epithelial cell differentiation
A	0031639	biological_process	plasminogen activation
A	0043531	molecular_function	ADP binding
A	0045121	cellular_component	membrane raft
A	0047134	molecular_function	protein-disulfide reductase (NAD(P)H) activity
A	0061621	biological_process	canonical glycolysis
A	0070062	cellular_component	extracellular exosome
A	0071456	biological_process	cellular response to hypoxia

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	binding site for residue MG A 501

Chain	Residue
A	ASP374
A	ADP503
A	HOH722
A	HOH732
A	HOH759

---

site_id	AC2
Number of Residues	16
Details	binding site for residue 3PG A 502

Chain	Residue
A	ARG65
A	ARG122
A	GLY166
A	ARG170
A	LYS215
A	HOH636
A	HOH650
A	HOH722
A	HOH726
A	HOH732
A	HOH741
A	HOH795
A	ASP23
A	ASN25
A	ARG38
A	HIS62

---

site_id	AC3
Number of Residues	30
Details	binding site for residue ADP A 503

Chain	Residue
A	GLY213
A	ALA214
A	LYS215
A	LYS219
A	GLY237
A	GLY238
A	PHE241
A	LEU256
A	GLY312
A	ASN336
A	PRO338
A	GLY340
A	VAL341
A	GLU343
A	GLY371
A	GLY372
A	GLY373
A	ASP374
A	THR375
A	MG501
A	HOH605
A	HOH636
A	HOH705
A	HOH722
A	HOH726
A	HOH729
A	HOH732
A	HOH754
A	HOH759
A	HOH799

---

site_id	AC4
Number of Residues	11
Details	binding site for residue BTB A 504

Chain	Residue
A	HIS169
A	GLN221
A	GLU293
A	ASN294
A	ALA295
A	THR297
A	ALA346
A	GLU400
A	LYS405
A	HOH602
A	HOH675

---

Functional Information from PROSITE/UniProt

site_id	PS00111
Number of Residues	11
Details	PGLYCERATE_KINASE Phosphoglycerate kinase signature. RVVMRvDfNVP

Chain	Residue	Details
A	ARG17-PRO27

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	BINDING: BINDING => ECO:0000269|PubMed:18463139

Chain	Residue	Details
A	ASP23
A	ARG38
A	HIS62
A	ARG122
A	ARG170
A	LYS219
A	GLY312
A	GLU343
A	GLY372

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER1
A	SER3

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	LYS5
A	LYS190

---

site_id	SWS_FT_FI4
Number of Residues	7
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS10
A	LYS74
A	LYS85
A	LYS145
A	LYS198
A	LYS266
A	LYS290

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	LYS47

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	TYR75

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P09411

Chain	Residue	Details
A	LYS90
A	LYS360

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS96

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: N6-malonyllysine; alternate => ECO:0000269|PubMed:21908771

Chain	Residue	Details
A	LYS130

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455

Chain	Residue	Details
A	TYR195

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	SER202

---

site_id	SWS_FT_FI12
Number of Residues	2
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581

Chain	Residue	Details
A	LYS215
A	LYS322

---

site_id	SWS_FT_FI13
Number of Residues	1
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29192674

Chain	Residue	Details
A	LYS219

---