Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4WMQ

Structure of Human Intelectin-1

Functional Information from GO Data
ChainGOidnamespacecontents
A0001934biological_processpositive regulation of protein phosphorylation
A0005509molecular_functioncalcium ion binding
A0005515molecular_functionprotein binding
A0005576cellular_componentextracellular region
A0005615cellular_componentextracellular space
A0005886cellular_componentplasma membrane
A0009624biological_processresponse to nematode
A0030246molecular_functioncarbohydrate binding
A0031526cellular_componentbrush border membrane
A0042802molecular_functionidentical protein binding
A0043235cellular_componentreceptor complex
A0045121cellular_componentmembrane raft
A0046326biological_processpositive regulation of glucose import
A0046872molecular_functionmetal ion binding
A0070062cellular_componentextracellular exosome
A0070207biological_processprotein homotrimerization
A0070492molecular_functionoligosaccharide binding
A0098552cellular_componentside of membrane
B0001934biological_processpositive regulation of protein phosphorylation
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005576cellular_componentextracellular region
B0005615cellular_componentextracellular space
B0005886cellular_componentplasma membrane
B0009624biological_processresponse to nematode
B0030246molecular_functioncarbohydrate binding
B0031526cellular_componentbrush border membrane
B0042802molecular_functionidentical protein binding
B0043235cellular_componentreceptor complex
B0045121cellular_componentmembrane raft
B0046326biological_processpositive regulation of glucose import
B0046872molecular_functionmetal ion binding
B0070062cellular_componentextracellular exosome
B0070207biological_processprotein homotrimerization
B0070492molecular_functionoligosaccharide binding
B0098552cellular_componentside of membrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CA A 401
ChainResidue
AHIS86
AGLY97
AASP133
AASP282
AHOH589
AHOH663

site_idAC2
Number of Residues6
Detailsbinding site for residue CA A 402
ChainResidue
AASP98
AHOH573
AHOH640
AGLU87
AASP89
AGLY92

site_idAC3
Number of Residues7
Detailsbinding site for residue CA A 403
ChainResidue
AASN260
AGLU262
AGLU274
AHOH534
AHOH611
AHOH619
AHOH632

site_idAC4
Number of Residues6
Detailsbinding site for residue CA B 401
ChainResidue
BHIS86
BGLY97
BASP133
BASP282
BHOH563
BHOH632

site_idAC5
Number of Residues6
Detailsbinding site for residue CA B 402
ChainResidue
BGLU87
BASP89
BGLY92
BASP98
BHOH581
BHOH582

site_idAC6
Number of Residues7
Detailsbinding site for residue CA B 403
ChainResidue
BASN260
BGLU262
BGLU274
BHOH534
BHOH558
BHOH578
BHOH605

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues22
DetailsBINDING: BINDING => ECO:0000269|PubMed:26148048, ECO:0007744|PDB:4WMQ, ECO:0007744|PDB:4WMY
ChainResidueDetails
AHIS86
AGLU274
AASP282
BHIS86
BGLU87
BASP89
BGLY92
BGLY97
BASP98
BASP133
BASN260
AGLU87
BGLU262
BGLU274
BASP282
AASP89
AGLY92
AGLY97
AASP98
AASP133
AASN260
AGLU262

site_idSWS_FT_FI2
Number of Residues2
DetailsLIPID: GPI-anchor amidated serine => ECO:0000255
ChainResidueDetails
ASER298
BSER298

site_idSWS_FT_FI3
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000305
ChainResidueDetails
AASN163
BASN163

222624

PDB entries from 2024-07-17

PDB statisticsPDBj update infoContact PDBjnumon