Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2W5A

Human Nek2 kinase ADP-bound

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues23
DetailsBINDING SITE FOR RESIDUE ADP A 1280
ChainResidue
AGLY17
AARG164
AMG1281
AHOH2034
AHOH2158
AHOH2159
AHOH2205
AHOH2207
AHOH2342
AHOH2343
AHOH2344
ASER18
AHOH2345
AHOH2346
AHOH2347
AHOH2348
ACYS22
ALYS37
AGLU87
ATYR88
ACYS89
AASP93
APHE148

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE MG A 1281
ChainResidue
ALYS37
AARG164
AADP1280
AHOH2207
AHOH2220
AHOH2221
AHOH2347

site_idAC3
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1282
ChainResidue
ALEU11
ALYS152
AGLN153
AHOH2337
AHOH2349
AHOH2350

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1283
ChainResidue
AHIS139
AARG140
AASP159
AHOH2110
AHOH2351
AHOH2352

site_idAC5
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 1284
ChainResidue
ALEU122
AARG235
AASP242
AHIS276
AHIS277
AHOH2109
AHOH2278
AHOH2353

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1285
ChainResidue
AGLU246
AILE247
AGLU264
AASN268

Functional Information from PROSITE/UniProt
site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDLKpaNVFL
ChainResidueDetails
AVAL137-LEU149

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues2
DetailsModified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"17197699","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AALA145
AASP141

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS143
AASP141

site_idCSA3
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR179
ALYS143
AASP141

site_idCSA4
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS143
AASP141
AASN146

246704

PDB entries from 2025-12-24

PDB statisticsPDBj update infoContact PDBjnumon