4O3F

Crystal Structure of mouse PGK1 3PG and terazosin(TZN) ternary complex

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	0005759	cellular_component	mitochondrial matrix
A	0005829	cellular_component	cytosol
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0016301	molecular_function	kinase activity
A	0016525	biological_process	negative regulation of angiogenesis
A	0030855	biological_process	epithelial cell differentiation
A	0031639	biological_process	plasminogen activation
A	0045121	cellular_component	membrane raft
A	0046166	biological_process	glyceraldehyde-3-phosphate biosynthetic process
A	0047134	molecular_function	protein-disulfide reductase (NAD(P)H) activity
A	0061621	biological_process	canonical glycolysis
A	0071456	biological_process	cellular response to hypoxia

Functional Information from PDB Data

site_id	AC1
Number of Residues	13
Details	BINDING SITE FOR RESIDUE TZN A 501

Chain	Residue
A	GLY214
A	GLY341
A	VAL342
A	HOH605
A	HOH804
A	GLY238
A	GLY239
A	THR255
A	LEU257
A	MET312
A	GLY313
A	LEU314
A	PRO339

---

site_id	AC2
Number of Residues	14
Details	BINDING SITE FOR RESIDUE 3PG A 502

Chain	Residue
A	ASP24
A	ASN26
A	ARG39
A	HIS63
A	ARG66
A	ARG123
A	GLY167
A	THR168
A	ARG171
A	HOH625
A	HOH644
A	HOH666
A	HOH700
A	HOH737

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	ARG18-PRO28

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	9
Details	BINDING: BINDING => ECO:0000250|UniProtKB:Q7SIB7

Chain	Residue	Details
A	ASP24
A	ARG39
A	HIS63
A	ARG123
A	ARG171
A	LYS220
A	GLY313
A	GLU344
A	GLY373

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	SER2
A	SER4

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337

Chain	Residue	Details
A	LYS6
A	LYS191

---

site_id	SWS_FT_FI4
Number of Residues	4
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:23806337

Chain	Residue	Details
A	LYS11
A	LYS91
A	LYS291
A	LYS361

---

site_id	SWS_FT_FI5
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337

Chain	Residue	Details
A	LYS48

---

site_id	SWS_FT_FI6
Number of Residues	5
Details	MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	LYS75
A	LYS86
A	LYS146
A	LYS199
A	LYS267

---

site_id	SWS_FT_FI7
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:18034455

Chain	Residue	Details
A	TYR76

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: N6-acetyllysine; alternate => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	LYS97

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: N6-malonyllysine; alternate => ECO:0000250

Chain	Residue	Details
A	LYS131

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	TYR196

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:19131326, ECO:0007744|PubMed:21183079

Chain	Residue	Details
A	SER203

---

site_id	SWS_FT_FI12
Number of Residues	3
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000250|UniProtKB:P00558

Chain	Residue	Details
A	LYS216
A	LYS220
A	LYS323

---