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3ME2

Crystal structure of mouse RANKL-RANK complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005164molecular_functiontumor necrosis factor receptor binding
A0006955biological_processimmune response
A0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues6
DetailsBINDING SITE FOR RESIDUE CL A 5
ChainResidue
ASER184
ASER185
ATRP186
ALEU200
AASN202
AGLY203

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 6
ChainResidue
AHIS188
AASP189
AARG190

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL A 7
ChainResidue
ALYS194
ALYS281
RLYS86

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NA R 1
ChainResidue
RCYS134
RALA135
RPHE138
RSER161
RVAL163
RHOH239

site_idAC5
Number of Residues3
DetailsBINDING SITE FOR RESIDUE CL R 219
ChainResidue
RHIS90
RLYS91
RARG111

Functional Information from PROSITE/UniProt
site_idPS00652
Number of Residues35
DetailsTNFR_NGFR_1 TNFR/NGFR family cysteine-rich region signature. Ctqerh.Yehlgr.....C..Csr.Cepgkylssk..Ctpts..DSVC
ChainResidueDetails
RCYS35-CYS69

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CaCtaGYhwnsdcecC
ChainResidueDetails
RCYS113-CYS128

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues5
DetailsBINDING:
ChainResidueDetails
RCYS134
RALA135
RPHE138
RSER161
RVAL163

site_idSWS_FT_FI2
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:23039992
ChainResidueDetails
RASN106

site_idSWS_FT_FI3
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
RASN175

219140

PDB entries from 2024-05-01

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