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1W6N

X-RAY CRYSTAL STRUCTURE OF C2S HUMAN GALECTIN-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0002317biological_processplasma cell differentiation
A0003723molecular_functionRNA binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005737cellular_componentcytoplasm
A0005788cellular_componentendoplasmic reticulum lumen
A0005829cellular_componentcytosol
A0005886cellular_componentplasma membrane
A0006915biological_processapoptotic process
A0007165biological_processsignal transduction
A0030246molecular_functioncarbohydrate binding
A0030395molecular_functionlactose binding
A0031295biological_processT cell costimulation
A0042981biological_processregulation of apoptotic process
A0043065biological_processpositive regulation of apoptotic process
A0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
A0043236molecular_functionlaminin binding
A0045445biological_processmyoblast differentiation
A0046598biological_processpositive regulation of viral entry into host cell
A0048018molecular_functionreceptor ligand activity
A0050729biological_processpositive regulation of inflammatory response
A0062023cellular_componentcollagen-containing extracellular matrix
A0070062cellular_componentextracellular exosome
A0098609biological_processcell-cell adhesion
A1990724cellular_componentgalectin complex
A2000329biological_processnegative regulation of T-helper 17 cell lineage commitment
A2001200biological_processpositive regulation of dendritic cell differentiation
B0002317biological_processplasma cell differentiation
B0003723molecular_functionRNA binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005737cellular_componentcytoplasm
B0005788cellular_componentendoplasmic reticulum lumen
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0006915biological_processapoptotic process
B0007165biological_processsignal transduction
B0030246molecular_functioncarbohydrate binding
B0030395molecular_functionlactose binding
B0031295biological_processT cell costimulation
B0042981biological_processregulation of apoptotic process
B0043065biological_processpositive regulation of apoptotic process
B0043123biological_processpositive regulation of canonical NF-kappaB signal transduction
B0043236molecular_functionlaminin binding
B0045445biological_processmyoblast differentiation
B0046598biological_processpositive regulation of viral entry into host cell
B0048018molecular_functionreceptor ligand activity
B0050729biological_processpositive regulation of inflammatory response
B0062023cellular_componentcollagen-containing extracellular matrix
B0070062cellular_componentextracellular exosome
B0098609biological_processcell-cell adhesion
B1990724cellular_componentgalectin complex
B2000329biological_processnegative regulation of T-helper 17 cell lineage commitment
B2001200biological_processpositive regulation of dendritic cell differentiation
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A2135
ChainResidue
APRO1109
AARG1111
AHOH2090
AHOH2091
AHOH2092
BARG2018
BLYS2099
BBME3135

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME A2136
ChainResidue
ACYS1088
ALYS1099
ALEU1100
AGLU1086

site_idAC3
Number of Residues2
DetailsBINDING SITE FOR RESIDUE BME A2137
ChainResidue
ACYS1130
AVAL1131

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE BME B3135
ChainResidue
AHOH2049
ASO42135
BCYS2016
BCYS2088
BILE2089

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE BME B3136
ChainResidue
BARG2018
BGLU2086
BCYS2088
BLYS2099
BLEU2100
BHOH4126

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE BME B3137
ChainResidue
BARG2018
BCYS2130
BVAL2131
BALA2132

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsBINDING:
ChainResidueDetails
BPHE2045
BGLY2053
BSER2062
BGLY2069

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: N-acetylalanine => ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378, ECO:0007744|PubMed:25944712
ChainResidueDetails
BSER2002

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P16045
ChainResidueDetails
BPRO2013
BILE2128

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861
ChainResidueDetails
BSER2029

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:26091039
ChainResidueDetails
BPHE2030

site_idSWS_FT_FI6
Number of Residues1
DetailsMOD_RES: N6-succinyllysine; alternate => ECO:0000250|UniProtKB:P16045
ChainResidueDetails
BPHE2108

229183

PDB entries from 2024-12-18

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