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6NDG

RHODOCETIN IN COMPLEX WITH THE INTEGRIN ALPHA2-A DOMAIN WITH YTTRIUM BOUND

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0035821biological_processmodulation of process of another organism
A0090729molecular_functiontoxin activity
B0005576cellular_componentextracellular region
B0035821biological_processmodulation of process of another organism
B0090729molecular_functiontoxin activity
D0005576cellular_componentextracellular region
D0035821biological_processmodulation of process of another organism
D0090729molecular_functiontoxin activity
E0005576cellular_componentextracellular region
E0035821biological_processmodulation of process of another organism
E0090729molecular_functiontoxin activity
G0005576cellular_componentextracellular region
G0035821biological_processmodulation of process of another organism
G0090729molecular_functiontoxin activity
H0005576cellular_componentextracellular region
H0035821biological_processmodulation of process of another organism
H0090729molecular_functiontoxin activity
J0005576cellular_componentextracellular region
J0035821biological_processmodulation of process of another organism
J0090729molecular_functiontoxin activity
K0005576cellular_componentextracellular region
K0035821biological_processmodulation of process of another organism
K0090729molecular_functiontoxin activity
M0005576cellular_componentextracellular region
M0035821biological_processmodulation of process of another organism
M0090729molecular_functiontoxin activity
N0005576cellular_componentextracellular region
N0035821biological_processmodulation of process of another organism
N0090729molecular_functiontoxin activity
P0005576cellular_componentextracellular region
P0035821biological_processmodulation of process of another organism
P0090729molecular_functiontoxin activity
Q0005576cellular_componentextracellular region
Q0035821biological_processmodulation of process of another organism
Q0090729molecular_functiontoxin activity
Functional Information from PDB Data
site_idAC1
Number of Residues3
Detailsbinding site for residue SO4 A 201
ChainResidue
APHE19
AASN20
AGLU21

site_idAC2
Number of Residues2
Detailsbinding site for residue SO4 A 202
ChainResidue
AARG73
AARG75

site_idAC3
Number of Residues7
Detailsbinding site for residue SO4 B 201
ChainResidue
CTHR250
CY1401
CNA402
BARG92
BLYS114
CSER184
CASP248

site_idAC4
Number of Residues5
Detailsbinding site for residue Y1 C 401
ChainResidue
BSO4201
CSER182
CSER184
CASP283
CNA402

site_idAC5
Number of Residues3
Detailsbinding site for residue NA C 402
ChainResidue
BSO4201
CSER184
CY1401

site_idAC6
Number of Residues2
Detailsbinding site for residue CL C 403
ChainResidue
CARG260
GGLY7

site_idAC7
Number of Residues2
Detailsbinding site for residue CL C 404
ChainResidue
CARG339
OARG339

site_idAC8
Number of Residues3
Detailsbinding site for residue SO4 D 201
ChainResidue
DPHE19
DASN20
DNH4202

site_idAC9
Number of Residues3
Detailsbinding site for residue NH4 D 202
ChainResidue
DGLN17
DALA18
DSO4201

site_idAD1
Number of Residues2
Detailsbinding site for residue SO4 E 201
ChainResidue
ELYS101
EARG104

site_idAD2
Number of Residues1
Detailsbinding site for residue CL E 202
ChainResidue
ELYS59

site_idAD3
Number of Residues4
Detailsbinding site for residue SO4 E 203
ChainResidue
ELYS114
FTHR250
FY1401
FNA402

site_idAD4
Number of Residues6
Detailsbinding site for residue Y1 F 401
ChainResidue
ESO4203
FASP180
FSER182
FSER184
FASP283
FNA402

site_idAD5
Number of Residues4
Detailsbinding site for residue NA F 402
ChainResidue
ESO4203
FSER182
FSER184
FY1401

site_idAD6
Number of Residues2
Detailsbinding site for residue SO4 G 201
ChainResidue
GPHE19
GASN20

site_idAD7
Number of Residues1
Detailsbinding site for residue CL H 201
ChainResidue
HLYS59

site_idAD8
Number of Residues4
Detailsbinding site for residue SO4 H 202
ChainResidue
HLYS114
ITHR250
IY1401
INA402

site_idAD9
Number of Residues7
Detailsbinding site for residue Y1 I 401
ChainResidue
HSO4202
IASP180
ISER182
ISER184
ITHR250
IASP283
INA402

site_idAE1
Number of Residues4
Detailsbinding site for residue NA I 402
ChainResidue
HSO4202
ISER182
ISER184
IY1401

site_idAE2
Number of Residues3
Detailsbinding site for residue SO4 J 201
ChainResidue
JPHE19
JASN20
JGLU21

site_idAE3
Number of Residues1
Detailsbinding site for residue CL J 202
ChainResidue
JARG73

site_idAE4
Number of Residues1
Detailsbinding site for residue CL K 201
ChainResidue
KARG14

site_idAE5
Number of Residues6
Detailsbinding site for residue SO4 K 202
ChainResidue
KARG92
KLYS114
LASP248
LTHR250
LY1401
LNA402

site_idAE6
Number of Residues5
Detailsbinding site for residue Y1 L 401
ChainResidue
KSO4202
LSER182
LSER184
LASP283
LNA402

site_idAE7
Number of Residues4
Detailsbinding site for residue NA L 402
ChainResidue
KSO4202
LSER182
LSER184
LY1401

site_idAE8
Number of Residues1
Detailsbinding site for residue CL L 403
ChainResidue
LARG260

site_idAE9
Number of Residues2
Detailsbinding site for residue CL M 201
ChainResidue
MGLN102
NARG91

site_idAF1
Number of Residues6
Detailsbinding site for residue SO4 N 201
ChainResidue
NARG92
NLYS114
OASP248
OTHR250
OY1401
ONA402

site_idAF2
Number of Residues6
Detailsbinding site for residue Y1 O 401
ChainResidue
ONA402
NSO4201
OSER182
OSER184
OTHR250
OASP283

site_idAF3
Number of Residues3
Detailsbinding site for residue NA O 402
ChainResidue
NSO4201
OSER184
OY1401

site_idAF4
Number of Residues3
Detailsbinding site for residue SO4 O 403
ChainResidue
OARG260
OLYS261
OGLN298

site_idAF5
Number of Residues2
Detailsbinding site for residue SO4 Q 201
ChainResidue
QTYR8
QASN9

site_idAF6
Number of Residues6
Detailsbinding site for residue SO4 Q 202
ChainResidue
QARG92
QLYS114
RASP248
RTHR250
RY1401
RNA404

site_idAF7
Number of Residues6
Detailsbinding site for residue Y1 R 401
ChainResidue
QSO4202
RSER182
RSER184
RTHR250
RASP283
RNA404

site_idAF8
Number of Residues4
Detailsbinding site for residue SO4 R 402
ChainResidue
RGLN257
RARG260
RLYS261
RGLN298

site_idAF9
Number of Residues4
Detailsbinding site for residue NA R 404
ChainResidue
QSO4202
RSER182
RSER184
RY1401

Functional Information from PROSITE/UniProt
site_idPS00615
Number of Residues26
DetailsC_TYPE_LECTIN_1 C-type lectin domain signature. CAvmvvktdrif..WFNRGCektvs.FVC
ChainResidueDetails
BCYS95-CYS120

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1392
DetailsDomain: {"description":"C-type lectin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00040","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"16263699","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19349973","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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