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3COH

Crystal structure of Aurora-A in complex with a pentacyclic inhibitor

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
B0004672molecular_functionprotein kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
Functional Information from PDB Data
site_idAC1
Number of Residues10
DetailsBINDING SITE FOR RESIDUE 83H A 1
ChainResidue
ALEU139
ALEU263
AALA160
ALEU194
AGLU211
ATYR212
AALA213
APRO214
ALEU215
AGLY216

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE 83H B 2
ChainResidue
BLEU139
BALA160
BLEU194
BGLU211
BTYR212
BALA213
BPRO214
BGLY216

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues24
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGKFGNVYlAreknskfi..........LALK
ChainResidueDetails
ALEU139-LYS162

site_idPS00108
Number of Residues13
DetailsPROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDIKpeNLLL
ChainResidueDetails
AVAL252-LEU264

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, ECO:0000269|PubMed:14580337
ChainResidueDetails
AASP256
BASP256

site_idSWS_FT_FI2
Number of Residues10
DetailsBINDING: BINDING => ECO:0000269|PubMed:27837025, ECO:0007744|PDB:5G1X
ChainResidueDetails
ALYS143
BASP274
ALYS162
AGLU211
AGLU260
AASP274
BLYS143
BLYS162
BGLU211
BGLU260

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:19668197
ChainResidueDetails
AALA287
BALA287

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0000269|PubMed:11039908, ECO:0000269|PubMed:13678582, ECO:0000269|PubMed:14580337, ECO:0000269|PubMed:16246726, ECO:0000269|PubMed:18662907, ECO:0000269|PubMed:19668197, ECO:0000269|PubMed:26246606
ChainResidueDetails
AALA288
BALA288

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphoserine; by PKA and PAK => ECO:0000269|PubMed:16246726
ChainResidueDetails
ASER342
BSER342

site_idSWS_FT_FI6
Number of Residues4
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) => ECO:0007744|PubMed:28112733
ChainResidueDetails
ALYS258
BLYS258

Catalytic Information from CSA
site_idCSA1
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
AASP256
AGLU260

site_idCSA2
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BASP256
BGLU260

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS258
AASP256

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS258
BASP256

site_idCSA5
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ATHR292
ALYS258
AASP256

site_idCSA6
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BTHR292
BLYS258
BASP256

site_idCSA7
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
ALYS258
AASN261
AASP256

site_idCSA8
Number of Residues3
DetailsAnnotated By Reference To The Literature 1ir3
ChainResidueDetails
BLYS258
BASN261
BASP256

223532

PDB entries from 2024-08-07

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