6F83

Crystal Structure of Human Galectin-1 in Complex With Thienyl-1,2, 3-triazolyl Thiodigalactoside Inhibitor

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002317	biological_process	plasma cell differentiation
A	0003723	molecular_function	RNA binding
A	0005515	molecular_function	protein binding
A	0005576	cellular_component	extracellular region
A	0005615	cellular_component	extracellular space
A	0005737	cellular_component	cytoplasm
A	0005788	cellular_component	endoplasmic reticulum lumen
A	0005829	cellular_component	cytosol
A	0005886	cellular_component	plasma membrane
A	0006915	biological_process	apoptotic process
A	0007165	biological_process	signal transduction
A	0030246	molecular_function	carbohydrate binding
A	0030395	molecular_function	lactose binding
A	0031012	cellular_component	extracellular matrix
A	0031295	biological_process	T cell costimulation
A	0042981	biological_process	regulation of apoptotic process
A	0043065	biological_process	positive regulation of apoptotic process
A	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
A	0043236	molecular_function	laminin binding
A	0045445	biological_process	myoblast differentiation
A	0046598	biological_process	positive regulation of viral entry into host cell
A	0048018	molecular_function	receptor ligand activity
A	0050729	biological_process	positive regulation of inflammatory response
A	0070062	cellular_component	extracellular exosome
A	0098609	biological_process	cell-cell adhesion
A	1990724	cellular_component	galectin complex
A	2000329	biological_process	negative regulation of T-helper 17 cell lineage commitment
A	2001200	biological_process	positive regulation of dendritic cell differentiation
B	0002317	biological_process	plasma cell differentiation
B	0003723	molecular_function	RNA binding
B	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005788	cellular_component	endoplasmic reticulum lumen
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006915	biological_process	apoptotic process
B	0007165	biological_process	signal transduction
B	0030246	molecular_function	carbohydrate binding
B	0030395	molecular_function	lactose binding
B	0031012	cellular_component	extracellular matrix
B	0031295	biological_process	T cell costimulation
B	0042981	biological_process	regulation of apoptotic process
B	0043065	biological_process	positive regulation of apoptotic process
B	0043123	biological_process	positive regulation of canonical NF-kappaB signal transduction
B	0043236	molecular_function	laminin binding
B	0045445	biological_process	myoblast differentiation
B	0046598	biological_process	positive regulation of viral entry into host cell
B	0048018	molecular_function	receptor ligand activity
B	0050729	biological_process	positive regulation of inflammatory response
B	0070062	cellular_component	extracellular exosome
B	0098609	biological_process	cell-cell adhesion
B	1990724	cellular_component	galectin complex
B	2000329	biological_process	negative regulation of T-helper 17 cell lineage commitment
B	2001200	biological_process	positive regulation of dendritic cell differentiation

Functional Information from PDB Data

site_id	AC1
Number of Residues	14
Details	binding site for residue 5KT A 201

Chain	Residue
A	SER29
A	ASP123
A	GLY124
A	HOH316
B	THR70
B	HOH327
A	VAL31
A	HIS44
A	ASN46
A	ARG48
A	HIS52
A	ASN61
A	GLU71
A	ARG73

---

site_id	AC2
Number of Residues	12
Details	binding site for residue 5KT B 201

Chain	Residue
A	GLN72
B	SER29
B	VAL31
B	HIS44
B	ASN46
B	ARG48
B	ASN61
B	GLU71
B	ARG73
B	ASP123
B	GLY124
B	HOH324

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	18
Details	Binding site: {}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"PubMed","id":"22223895","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"25944712","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P16045","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine; by FAM20C","evidences":[{"source":"PubMed","id":"26091039","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P16045","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---