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4UHZ

Crystal structure of the human RGMB-BMP2 complex, crystal form 1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008083molecular_functiongrowth factor activity
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1123
ChainResidue
BCYS82
BARG86
BASN120
BCYS121

site_idAC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1397
ChainResidue
ASER294
ASER295
ALYS297

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE SO4 A 1398
ChainResidue
ALYS358
AASN350
ASER354

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 B 1124
ChainResidue
ALYS383
BGLN53
BCYS54
BASN102

site_idAC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE SO4 A 1399
ChainResidue
AASN341
AASN384
ATYR385
AGLN386

site_idAC6
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 1400
ChainResidue
AHIS321

site_idAC7
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 1401
ChainResidue
AARG298

site_idAC8
Number of Residues1
DetailsBINDING SITE FOR RESIDUE SO4 A 1402
ChainResidue
ASER294

Functional Information from PROSITE/UniProt
site_idPS00250
Number of Residues16
DetailsTGF_BETA_1 TGF-beta family signature. IvaPpgYhafyChGeC
ChainResidueDetails
AILE314-CYS329

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"9265423","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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