4GA9

Crystal Structure of Rat Galectin-1 in Complex with Lactose

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002317	biological_process	plasma cell differentiation
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	0006915	biological_process	apoptotic process
A	0007165	biological_process	signal transduction
A	0009410	biological_process	response to xenobiotic stimulus
A	0009986	cellular_component	cell surface
A	0010812	biological_process	negative regulation of cell-substrate adhesion
A	0010977	biological_process	negative regulation of neuron projection development
A	0030246	molecular_function	carbohydrate binding
A	0030395	molecular_function	lactose binding
A	0031295	biological_process	T cell costimulation
A	0034120	biological_process	positive regulation of erythrocyte aggregation
A	0035900	biological_process	response to isolation stress
A	0042802	molecular_function	identical protein binding
A	0043065	biological_process	positive regulation of apoptotic process
A	0043236	molecular_function	laminin binding
A	0045185	biological_process	maintenance of protein location
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	0048678	biological_process	response to axon injury
A	0050729	biological_process	positive regulation of inflammatory response
A	0071333	biological_process	cellular response to glucose stimulus
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	0005515	molecular_function	protein binding
B	0005576	cellular_component	extracellular region
B	0005615	cellular_component	extracellular space
B	0005737	cellular_component	cytoplasm
B	0005829	cellular_component	cytosol
B	0005886	cellular_component	plasma membrane
B	0006915	biological_process	apoptotic process
B	0007165	biological_process	signal transduction
B	0009410	biological_process	response to xenobiotic stimulus
B	0009986	cellular_component	cell surface
B	0010812	biological_process	negative regulation of cell-substrate adhesion
B	0010977	biological_process	negative regulation of neuron projection development
B	0030246	molecular_function	carbohydrate binding
B	0030395	molecular_function	lactose binding
B	0031295	biological_process	T cell costimulation
B	0034120	biological_process	positive regulation of erythrocyte aggregation
B	0035900	biological_process	response to isolation stress
B	0042802	molecular_function	identical protein binding
B	0043065	biological_process	positive regulation of apoptotic process
B	0043236	molecular_function	laminin binding
B	0045185	biological_process	maintenance of protein location
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	0048678	biological_process	response to axon injury
B	0050729	biological_process	positive regulation of inflammatory response
B	0071333	biological_process	cellular response to glucose stimulus
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 SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	262
Details	Domain: {"description":"Galectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00639","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	18
Details	Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI3
Number of Residues	2
Details	Modified residue: {"description":"N-acetylalanine","evidences":[{"source":"UniProtKB","id":"P09382","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI4
Number of Residues	6
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P16045","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI5
Number of Residues	2
Details	Modified residue: {"description":"N6-acetyllysine","evidences":[{"source":"UniProtKB","id":"P09382","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI6
Number of Residues	2
Details	Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P09382","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI7
Number of Residues	2
Details	Modified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P16045","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

---