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4UI1

Crystal structure of the human RGMC-BMP2 complex

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0008083molecular_functiongrowth factor activity
B0005576cellular_componentextracellular region
B0008083molecular_functiongrowth factor activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 1397
ChainResidue
BPHE331
BPRO332
BLEU333
BALA334
BILE344
BHOH2029
CSER105

site_idAC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE NO3 B 1398
ChainResidue
BALA359
BHOH2014
BGLU328
BCYS329

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE NO3 D 1130
ChainResidue
BASP375
BGLU376
BGLU378
DLEU53
DARG98

site_idAC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NO3 A 1397
ChainResidue
ATHR340
AASN341
BASP387

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE NO3 B 1399
ChainResidue
AASN341
BLYS383
BTYR385
BHOH2030
DASP100
DLEU101

site_idAC6
Number of Residues7
DetailsBINDING SITE FOR RESIDUE NO3 B 1400
ChainResidue
ACYS325
ACYS361
AHOH2012
BGLN346
BLYS358
BCYS360
BARG396

site_idAC7
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1398
ChainResidue
APRO332
ALEU333

site_idAC8
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CL A 1399
ChainResidue
ALYS383
CLEU101

site_idAC9
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1401
ChainResidue
AGLN346
AARG396
BTYR324
BCYS325
BCYS361
BPRO363

site_idBC1
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO C 1129
ChainResidue
CCYS80
CARG84
CSER120

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO D 1131
ChainResidue
AALA316
ASER370
DARG41

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 Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) (high mannose) asparagine","evidences":[{"source":"PubMed","id":"9265423","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"Q7TQ32","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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