1NUH

The crystal structure of human phosphoglucose isomerase complexed with 5-phosphoarabinonate

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0001701	biological_process	in utero embryonic development
A	0001707	biological_process	mesoderm formation
A	0002639	biological_process	positive regulation of immunoglobulin production
A	0004347	molecular_function	glucose-6-phosphate isomerase activity
A	0005125	molecular_function	cytokine activity
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0005975	biological_process	carbohydrate metabolic process
A	0006002	biological_process	fructose 6-phosphate metabolic process
A	0006094	biological_process	gluconeogenesis
A	0006096	biological_process	glycolytic process
A	0006959	biological_process	humoral immune response
A	0007165	biological_process	signal transduction
A	0007599	biological_process	hemostasis
A	0007611	biological_process	learning or memory
A	0008083	molecular_function	growth factor activity
A	0010595	biological_process	positive regulation of endothelial cell migration
A	0016020	cellular_component	membrane
A	0016853	molecular_function	isomerase activity
A	0031625	molecular_function	ubiquitin protein ligase binding
A	0032355	biological_process	response to estradiol
A	0032570	biological_process	response to progesterone
A	0033574	biological_process	response to testosterone
A	0034101	biological_process	erythrocyte homeostasis
A	0034774	cellular_component	secretory granule lumen
A	0035902	biological_process	response to immobilization stress
A	0035994	biological_process	response to muscle stretch
A	0042593	biological_process	glucose homeostasis
A	0043524	biological_process	negative regulation of neuron apoptotic process
A	0046686	biological_process	response to cadmium ion
A	0048029	molecular_function	monosaccharide binding
A	0051156	biological_process	glucose 6-phosphate metabolic process
A	0060170	cellular_component	ciliary membrane
A	0070062	cellular_component	extracellular exosome
A	0097367	molecular_function	carbohydrate derivative binding
A	0141199	biological_process	GDP-mannose biosynthetic process from glucose
A	1901135	biological_process	carbohydrate derivative metabolic process
A	1904813	cellular_component	ficolin-1-rich granule lumen

Functional Information from PDB Data

site_id	AC1
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 558

Chain	Residue
A	THR368
A	ARG369

---

site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 559

Chain	Residue
A	ARG27
A	ASN46
A	HIS47

---

site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 560

Chain	Residue
A	ARG136
A	HOH626

---

site_id	AC4
Number of Residues	3
Details	BINDING SITE FOR RESIDUE SO4 A 561

Chain	Residue
A	LYS240
A	TRP140
A	LYS141

---

site_id	AC5
Number of Residues	4
Details	BINDING SITE FOR RESIDUE SO4 A 562

Chain	Residue
A	TYR173
A	LYS480
A	THR482
A	HOH670

---

site_id	AC6
Number of Residues	2
Details	BINDING SITE FOR RESIDUE SO4 A 563

Chain	Residue
A	THR149
A	ARG179

---

site_id	AC7
Number of Residues	14
Details	BINDING SITE FOR RESIDUE PA5 A 564

Chain	Residue
A	ILE156
A	GLY157
A	GLY158
A	SER159
A	SER209
A	LYS210
A	THR211
A	THR214
A	GLN353
A	GLU357
A	HIS388
A	LYS518
A	HOH566
A	HOH601

---

Functional Information from PROSITE/UniProt

site_id	PS00174
Number of Residues	18
Details	P_GLUCOSE_ISOMERASE_2 Phosphoglucose isomerase signature 2. GiIWdinsFDQwGVElgK

Chain	Residue	Details
A	GLY501-LYS518

---

site_id	PS00765
Number of Residues	14
Details	P_GLUCOSE_ISOMERASE_1 Phosphoglucose isomerase signature 1. DwVGGRYSLwSAIG

Chain	Residue	Details
A	ASP267-GLY280

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	1
Details	ACT_SITE: Proton donor => ECO:0000269|PubMed:11371164, ECO:0000269|PubMed:12573240, ECO:0000269|PubMed:12777791

Chain	Residue	Details
A	GLU357

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:11371164, ECO:0000269|PubMed:12573240, ECO:0000269|PubMed:12777791

Chain	Residue	Details
A	HIS388
A	LYS518

---

site_id	SWS_FT_FI3
Number of Residues	6
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P06745

Chain	Residue	Details
A	GLY158
A	SER209
A	GLN353
A	GLU357
A	HIS388
A	LYS518

---

site_id	SWS_FT_FI4
Number of Residues	1
Details	MOD_RES: N-acetylalanine => ECO:0000269|Ref.8, ECO:0007744|PubMed:19413330

Chain	Residue	Details
A	ALA1

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861

Chain	Residue	Details
A	LYS11
A	LYS141

---

site_id	SWS_FT_FI6
Number of Residues	1
Details	MOD_RES: N6-(2-hydroxyisobutyryl)lysine => ECO:0000269|PubMed:29775581

Chain	Residue	Details
A	LYS33

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	MOD_RES: Phosphoserine => ECO:0007744|PubMed:23186163

Chain	Residue	Details
A	SER106
A	SER454

---

site_id	SWS_FT_FI8
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569

Chain	Residue	Details
A	THR108

---

site_id	SWS_FT_FI9
Number of Residues	1
Details	MOD_RES: Phosphoserine; by CK2 => ECO:0000269|PubMed:11004567, ECO:0000269|PubMed:15637053

Chain	Residue	Details
A	SER184

---

site_id	SWS_FT_FI10
Number of Residues	1
Details	MOD_RES: Phosphothreonine => ECO:0000250|UniProtKB:Q6P6V0

Chain	Residue	Details
A	THR249

---

site_id	SWS_FT_FI11
Number of Residues	1
Details	MOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P06745

Chain	Residue	Details
A	LYS453

---

Catalytic Information from CSA

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

Chain	Residue	Details
A	ARG272
A	LYS518
A	GLU216
A	GLU357
A	LYS210
A	GLY271

---

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

Chain	Residue	Details
A	HIS388

---