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5NB0

Crystal structures of homooligomers of collagen type IV. alpha3NC1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005201molecular_functionextracellular matrix structural constituent
A0005581cellular_componentcollagen trimer
B0005201molecular_functionextracellular matrix structural constituent
B0005581cellular_componentcollagen trimer
C0005201molecular_functionextracellular matrix structural constituent
C0005581cellular_componentcollagen trimer
D0005201molecular_functionextracellular matrix structural constituent
D0005581cellular_componentcollagen trimer
E0005201molecular_functionextracellular matrix structural constituent
E0005581cellular_componentcollagen trimer
F0005201molecular_functionextracellular matrix structural constituent
F0005581cellular_componentcollagen trimer
G0005201molecular_functionextracellular matrix structural constituent
G0005581cellular_componentcollagen trimer
H0005201molecular_functionextracellular matrix structural constituent
H0005581cellular_componentcollagen trimer
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CL A 301
ChainResidue
AALA74
AARG76
AASP78
AGLY178

site_idAC2
Number of Residues4
Detailsbinding site for residue CL A 302
ChainResidue
ATYR185
ASER186
DASN66
FTYR189

site_idAC3
Number of Residues4
Detailsbinding site for residue CL A 303
ChainResidue
BTYR189
DTYR185
DSER186
AASN66

site_idAC4
Number of Residues4
Detailsbinding site for residue CL B 301
ChainResidue
BALA74
BARG76
BASP78
BGLY178

site_idAC5
Number of Residues4
Detailsbinding site for residue CL B 302
ChainResidue
BTYR185
BSER186
DTYR189
EASN66

site_idAC6
Number of Residues4
Detailsbinding site for residue CL B 303
ChainResidue
BASN66
CTYR189
ETYR185
ESER186

site_idAC7
Number of Residues4
Detailsbinding site for residue CL C 301
ChainResidue
CMET60
CALA74
CARG76
CASP78

site_idAC8
Number of Residues5
Detailsbinding site for residue CL C 302
ChainResidue
CTYR185
CSER186
ETYR189
FPHE64
FASN66

site_idAC9
Number of Residues4
Detailsbinding site for residue CL D 301
ChainResidue
DALA74
DARG76
DASP78
DGLY178

site_idAD1
Number of Residues4
Detailsbinding site for residue CL E 301
ChainResidue
EMET60
EALA74
EARG76
EASP78

site_idAD2
Number of Residues5
Detailsbinding site for residue CL F 301
ChainResidue
FMET60
FALA74
FARG76
FASP78
FGLY178

site_idAD3
Number of Residues4
Detailsbinding site for residue CL F 302
ChainResidue
ATYR189
CASN66
FTYR185
FSER186

site_idAD4
Number of Residues4
Detailsbinding site for residue CL G 301
ChainResidue
GALA74
GARG76
GASP78
GGLY178

site_idAD5
Number of Residues3
Detailsbinding site for residue CL G 302
ChainResidue
GSER186
HASN66
HTYR189

site_idAD6
Number of Residues4
Detailsbinding site for residue CL G 303
ChainResidue
GPHE64
GASN66
GTYR189
HTYR185

site_idAD7
Number of Residues5
Detailsbinding site for residue CL H 301
ChainResidue
HALA74
HARG76
HASP78
HGLY178
HHOH427

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues8
DetailsCROSSLNK: S-Lysyl-methionine sulfilimine (Met-Lys) (interchain with K-1651) => ECO:0000250
ChainResidueDetails
AMET93
BMET93
CMET93
DMET93
EMET93
FMET93
GMET93
HMET93

site_idSWS_FT_FI2
Number of Residues16
DetailsCROSSLNK: S-Lysyl-methionine sulfilimine (Lys-Met) (interchain with M-1533) => ECO:0000250
ChainResidueDetails
ELYS211
FLYS211
GLYS211
HLYS211
ALYS211
BLYS211
CLYS211
DLYS211

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PDB entries from 2024-10-30

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