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6BXI

X-ray crystal structure of NDR1 kinase domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004674molecular_functionprotein serine/threonine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0004674molecular_functionprotein serine/threonine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues28
Detailsbinding site for residue ANP A 501
ChainResidue
AGLY96
AASP173
AASP216
AASN217
ALEU219
ASER229
AASP230
ACYS234
APHE410
AMG502
AHOH608
AGLY98
AHOH612
AHOH626
AHOH651
AHOH681
AHOH689
AHOH696
AHOH700
AHOH705
AHOH742
AVAL103
AALA116
ALYS118
AVAL150
AMET166
AGLU167
ALEU169

site_idAC2
Number of Residues3
Detailsbinding site for residue MG A 502
ChainResidue
AASN217
AANP501
AHOH700

site_idAC3
Number of Residues31
Detailsbinding site for residue ANP B 501
ChainResidue
BILE95
BGLY96
BGLY98
BVAL103
BALA116
BLYS118
BVAL150
BMET166
BGLU167
BLEU169
BASP173
BASP216
BASN217
BLEU219
BSER229
BASP230
BCYS234
BPHE410
BMG502
BHOH615
BHOH619
BHOH620
BHOH625
BHOH628
BHOH647
BHOH655
BHOH659
BHOH663
BHOH679
BHOH708
BHOH711

site_idAC4
Number of Residues4
Detailsbinding site for residue MG B 502
ChainResidue
BASN217
BANP501
BHOH620
BHOH659

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVRlVqkkdtghv..........YAMK
ChainResidueDetails
AILE95-LYS118

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FiHrDIKpdNLLL
ChainResidueDetails
APHE208-LEU220

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
ChainResidueDetails
AASP212
BASP212

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:O95835, ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AILE95
BILE95

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:12493777, ECO:0000269|PubMed:7761441
ChainResidueDetails
ALYS118
BLYS118

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER264
BSER264

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:12493777
ChainResidueDetails
ASER281
BSER281

223166

PDB entries from 2024-07-31

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