Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

4F4J

Conversion of the enzyme guanylate kinase into a mitotic spindle orienting protein by a single mutation that inhibits gmp- induced closing

Replaces:  3SQK
Functional Information from GO Data
ChainGOidnamespacecontents
A0004385molecular_functionguanylate kinase activity
A0005524molecular_functionATP binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005829cellular_componentcytosol
A0006163biological_processpurine nucleotide metabolic process
A0016301molecular_functionkinase activity
A0046037biological_processGMP metabolic process
A0046711biological_processGDP biosynthetic process
B0004385molecular_functionguanylate kinase activity
B0005524molecular_functionATP binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005829cellular_componentcytosol
B0006163biological_processpurine nucleotide metabolic process
B0016301molecular_functionkinase activity
B0046037biological_processGMP metabolic process
B0046711biological_processGDP biosynthetic process
Functional Information from PDB Data
site_idAC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE SO4 A 201
ChainResidue
ASER11
AGLY12
ATHR13
AGLY14
ALYS15
ASER16
BALA43
BGLY44

site_idAC2
Number of Residues6
DetailsBINDING SITE FOR RESIDUE SO4 B 201
ChainResidue
BGLY12
BTHR13
BGLY14
BLYS15
BSER16
BSER11

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 202
ChainResidue
ATHR40
AARG42
AASN77
BSER11
BARG147

site_idAC4
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 203
ChainResidue
AGLU142
ALYS146
BSER55
BVAL56
BHOH331

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 204
ChainResidue
BSER0
BPHE74
BSER75
BASN115
BHOH320

Functional Information from PROSITE/UniProt
site_idPS00856
Number of Residues18
DetailsGUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRtpRagEvnGkdYnFV
ChainResidueDetails
ATHR37-VAL54

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00100
ChainResidueDetails
AGLY9
BGLY9

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000269|PubMed:1314905, ECO:0000269|PubMed:1967656, ECO:0007744|PDB:1GKY
ChainResidueDetails
APRO35
BGLU70
BTYR79
BASP101
AARG39
ATYR51
AGLU70
ATYR79
AASP101
BPRO35
BARG39
BTYR51

site_idSWS_FT_FI3
Number of Residues2
DetailsMOD_RES: N-acetylserine => ECO:0000269|PubMed:1314905, ECO:0000269|PubMed:2551688
ChainResidueDetails
ASER2
BSER2

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER149
BSER149

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ATYR157
BTYR157

219140

PDB entries from 2024-05-01

PDB statisticsPDBj update infoContact PDBjnumon