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4FIF

Catalytic domain of human PAK4 with RPKPLVDP peptide

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 Residues19
DetailsBINDING SITE FOR RESIDUE ANP A 1000
ChainResidue
AGLU329
AGLU396
ALEU398
ALEU447
AASP458
APHE459
AGLY460
APHE461
AHOH1118
AHOH1119
AHOH1125
AGLY330
ASER331
ATHR332
AVAL335
AALA348
ALYS350
AGLU366
AMET395

site_idAC2
Number of Residues20
DetailsBINDING SITE FOR RESIDUE ANP B 1000
ChainResidue
BGLU329
BGLY330
BSER331
BTHR332
BVAL335
BALA348
BLYS350
BGLU366
BMET395
BGLU396
BPHE397
BLEU398
BLEU447
BASP458
BPHE459
BGLY460
BPHE461
BHOH1118
BHOH1119
BHOH1130

site_idAC3
Number of Residues13
DetailsBINDING SITE FOR CHAIN C OF SERINE/THREONINE-PROTEIN KINASE PAK 4
ChainResidue
ASER331
AGLN358
AARG359
ATHR404
ASER443
AASP444
APHE461
ALEU475
AVAL476
AGLY477
ATYR480
ATRP481
AGLU507

site_idAC4
Number of Residues12
DetailsBINDING SITE FOR CHAIN D OF SERINE/THREONINE-PROTEIN KINASE PAK 4
ChainResidue
BSER331
BARG359
BTHR404
BASP444
BLEU475
BVAL476
BGLY477
BPRO479
BTYR480
BTRP481
BGLU507
BPHE516

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues25
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGSTGIVCiAtvrssgklv.........AVKK
ChainResidueDetails
AILE327-LYS351

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
AASP440
BASP440

site_idSWS_FT_FI2
Number of Residues4
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:26607847, ECO:0007744|PDB:4XBR, ECO:0007744|PDB:4XBU
ChainResidueDetails
BILE327
BLYS350
AILE327
ALYS350

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:26607847, ECO:0007744|PDB:4XBR, ECO:0007744|PDB:4XBU
ChainResidueDetails
BGLU396
BASP458
AGLU396
AASP458

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:23186163
ChainResidueDetails
APRO314
BPRO314

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: N6-methyllysine => ECO:0007744|PubMed:24129315
ChainResidueDetails
ALYS351
BLYS351

site_idSWS_FT_FI6
Number of Residues10
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195
ChainResidueDetails
AASP440
ALEU531
ASER291
BASN377
BCYS421
BASP440
BLEU531
BSER291
AASN377
ACYS421

site_idSWS_FT_FI7
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569
ChainResidueDetails
AVAL454
BVAL454

site_idSWS_FT_FI8
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19369195
ChainResidueDetails
AGLY460
BGLY460

site_idSWS_FT_FI9
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
AGLU468
BGLU468

site_idSWS_FT_FI10
Number of Residues2
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163
ChainResidueDetails
ATYR480
BTYR480

site_idSWS_FT_FI11
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976
ChainResidueDetails
ALYS540
BLYS540

site_idSWS_FT_FI12
Number of Residues2
DetailsMOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|Ref.32, ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASEP474
BSEP474

219869

PDB entries from 2024-05-15

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