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6RFK

Crystal structure of EGRCK-inhibited Gla-domainless fIXa (K148Q, R150Q variant)

Functional Information from GO Data
ChainGOidnamespacecontents
S0004252molecular_functionserine-type endopeptidase activity
S0006508biological_processproteolysis
Functional Information from PDB Data
site_idAC1
Number of Residues15
Detailsbinding site for residue B3P E 201
ChainResidue
EASN92
EHOH310
SGLU204
SGOL303
SHOH402
SHOH497
SHOH591
EARG94
ECYS95
EGLU96
ELYS122
ESER123
EHOH301
EHOH308
EHOH309

site_idAC2
Number of Residues6
Detailsbinding site for residue CA S 301
ChainResidue
SGLU70
SASN72
SGLU75
SGLU77
SGLU80
SGOL308

site_idAC3
Number of Residues7
Detailsbinding site for residue GOL S 302
ChainResidue
ECYS88
ECYS99
SGLU127
STYR128
SILE129
SARG170
SHOH467

site_idAC4
Number of Residues8
Detailsbinding site for residue GOL S 303
ChainResidue
EB3P201
SHIS185
SGLU202
SVAL203
SGLU204
SHOH402
SHOH483
SHOH486

site_idAC5
Number of Residues7
Detailsbinding site for residue GOL S 304
ChainResidue
SGLY35
SLYS37
SVAL38
SPHE41
SCYS58
SVAL62
SLYS63

site_idAC6
Number of Residues7
Detailsbinding site for residue GOL S 305
ChainResidue
SASN97
STYR99
SPHE174
STHR175
STYR177
STRP215
SHOH507

site_idAC7
Number of Residues6
Detailsbinding site for residue GOL S 306
ChainResidue
SSER171
STHR172
SGLY216
SGLU217
SLYS224
STYR225

site_idAC8
Number of Residues3
Detailsbinding site for residue GOL S 307
ChainResidue
SASP21
SLEU153
SVAL154

site_idAC9
Number of Residues7
Detailsbinding site for residue GOL S 308
ChainResidue
SGLU70
SASN72
SILE73
SGLU75
SGLU80
SCA301
SHOH489

site_idAD1
Number of Residues5
Detailsbinding site for residue GOL S 309
ChainResidue
SHIS91
SASN93
SHIS101
SARG233
SHOH510

site_idAD2
Number of Residues9
Detailsbinding site for residue GOL S 310
ChainResidue
SLYS126
SASN129
SLYS230
SSER232
SARG233
SHOH405
SHOH407
SHOH546
SHOH549

site_idAD3
Number of Residues6
Detailsbinding site for residue GOL S 311
ChainResidue
SLYS132
SLEU162
SASP164
SASP164
SHOH401
SHOH401

site_idAD4
Number of Residues18
Detailsbinding site for residues AR7 I 3 and 0QE I 4
ChainResidue
SGLU219
SCYS220
SGLY226
SHOH442
SHOH499
IGLU1
IGLY2
IHOH102
SHIS57
SASP189
SSER190
SCYS191
SGLN192
SGLY193
SSER195
SSER214
STRP215
SGLY216

Functional Information from PROSITE/UniProt
site_idPS00134
Number of Residues6
DetailsTRYPSIN_HIS Serine proteases, trypsin family, histidine active site. VTAAHC
ChainResidueDetails
SVAL53-CYS58

site_idPS00135
Number of Residues12
DetailsTRYPSIN_SER Serine proteases, trypsin family, serine active site. DScqGDSGGPHV
ChainResidueDetails
SASP189-VAL200

site_idPS01186
Number of Residues16
DetailsEGF_2 EGF-like domain signature 2. CsCteGYrlaenqksC
ChainResidueDetails
ECYS109-CYS124

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:659613
ChainResidueDetails
SSER195
SHIS57

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: Charge relay system => ECO:0000269|PubMed:659613
ChainResidueDetails
SASP102

site_idSWS_FT_FI3
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:1RFN, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5
ChainResidueDetails
SGLU70
SGLU75
SGLU77
SASN72

site_idSWS_FT_FI4
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:10467148, ECO:0000269|PubMed:20004170, ECO:0000269|PubMed:20080729, ECO:0000269|PubMed:20121197, ECO:0000269|PubMed:20121198, ECO:0007744|PDB:2WPH, ECO:0007744|PDB:2WPI, ECO:0007744|PDB:2WPJ, ECO:0007744|PDB:2WPK, ECO:0007744|PDB:2WPM, ECO:0007744|PDB:3KCG, ECO:0007744|PDB:3LC3, ECO:0007744|PDB:3LC5
ChainResidueDetails
SGLU80

218500

PDB entries from 2024-04-17

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