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4YBH

Crystal structure of the human RAGE ectodomain (VC1C2 fragment) in complex with human S100A6

Functional Information from GO Data
ChainGOidnamespacecontents
B0001726cellular_componentruffle
B0005509molecular_functioncalcium ion binding
B0005515molecular_functionprotein binding
B0005523molecular_functiontropomyosin binding
B0005576cellular_componentextracellular region
B0005634cellular_componentnucleus
B0005635cellular_componentnuclear envelope
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0005886cellular_componentplasma membrane
B0007165biological_processsignal transduction
B0007409biological_processaxonogenesis
B0008270molecular_functionzinc ion binding
B0009898cellular_componentcytoplasmic side of plasma membrane
B0015075molecular_functionmonoatomic ion transmembrane transporter activity
B0031012cellular_componentextracellular matrix
B0034220biological_processmonoatomic ion transmembrane transport
B0042802molecular_functionidentical protein binding
B0042803molecular_functionprotein homodimerization activity
B0044548molecular_functionS100 protein binding
B0046872molecular_functionmetal ion binding
B0048146biological_processpositive regulation of fibroblast proliferation
B0048306molecular_functioncalcium-dependent protein binding
B0048471cellular_componentperinuclear region of cytoplasm
B0070062cellular_componentextracellular exosome
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue ZN A 401
ChainResidue
AASP160
AASP201
ACL406
ACL407

site_idAC2
Number of Residues3
Detailsbinding site for residue ZN A 402
ChainResidue
AASP128
AHIS180
AGLU182

site_idAC3
Number of Residues4
Detailsbinding site for residue ZN A 403
ChainResidue
AHOH507
AHOH550
AGLU32
AHIS217

site_idAC4
Number of Residues3
Detailsbinding site for residue ZN A 404
ChainResidue
AHIS270
ACL408
AHOH544

site_idAC5
Number of Residues6
Detailsbinding site for residue CL A 405
ChainResidue
AGLU132
AARG228
AZN412
BPHE16
BHIS17
BHIS27

site_idAC6
Number of Residues4
Detailsbinding site for residue CL A 406
ChainResidue
AASP160
AASP201
AZN401
ACL407

site_idAC7
Number of Residues6
Detailsbinding site for residue CL A 407
ChainResidue
AASP160
AASP201
AZN401
ACL406
AHOH640
BHOH206

site_idAC8
Number of Residues2
Detailsbinding site for residue CL A 408
ChainResidue
AHIS270
AZN404

site_idAC9
Number of Residues1
Detailsbinding site for residue ACT A 409
ChainResidue
ALYS169

site_idAD1
Number of Residues4
Detailsbinding site for residue ACT A 410
ChainResidue
AARG77
ALEU79
AVAL302
ATHR304

site_idAD2
Number of Residues4
Detailsbinding site for residue ACT A 411
ChainResidue
ATHR55
AARG57
ATRP72
AASP93

site_idAD3
Number of Residues4
Detailsbinding site for residue ZN A 412
ChainResidue
AGLU132
ACL405
BHIS17
BHIS27

site_idAD4
Number of Residues5
Detailsbinding site for residue ZN B 101
ChainResidue
BCYS3
BARG55
BASP59
BHOH201
BHOH205

site_idAD5
Number of Residues2
Detailsbinding site for residue ZN B 102
ChainResidue
BGLU41
BCL103

site_idAD6
Number of Residues2
Detailsbinding site for residue CL B 103
ChainResidue
BGLU41
BZN102

site_idAD7
Number of Residues6
Detailsbinding site for residue CA B 104
ChainResidue
BSER20
BGLU23
BASP25
BTHR28
BGLU33
BHOH207

site_idAD8
Number of Residues6
Detailsbinding site for residue CA B 105
ChainResidue
BASP61
BASN63
BASP65
BGLU67
BGLU72
BHOH224

Functional Information from PROSITE/UniProt
site_idPS00018
Number of Residues13
DetailsEF_HAND_1 EF-hand calcium-binding domain. DRNKDQEVNfqEY
ChainResidueDetails
BASP61-TYR73

site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YSCVATH
ChainResidueDetails
ATYR299-HIS305

site_idPS00303
Number of Residues22
DetailsS100_CABP S-100/ICaBP type calcium binding protein signature. LMedLDrnkDqevNFqEYvtFL
ChainResidueDetails
BLEU56-LEU77

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues93
DetailsDomain: {"description":"Ig-like V-type"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues97
DetailsDomain: {"description":"Ig-like C2-type 1"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues90
DetailsDomain: {"description":"Ig-like C2-type 2"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues35
DetailsDomain: {"description":"EF-hand 1","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues35
DetailsDomain: {"description":"EF-hand 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00448","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"N6-acetyllysine","evidences":[{"source":"PubMed","id":"19608861","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsModified residue: {"description":"N6-succinyllysine; alternate","evidences":[{"source":"UniProtKB","id":"P14069","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242199

PDB entries from 2025-09-24

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